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2,3-dimethyl-1,4-naphthoquinol + fumarate
?
-
-
-
-
?
D-malate + N,N,N',N'-tetramethyl 4-phenylenediamine
oxaloacetate + reduced N,N,N',N'-tetramethyl 4-phenylenediamine
-
-
-
-
r
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
succinate + 2,3-dimethyl-1,4-naphthoquinone
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
?
fumarate + 8-methylmenaquinol-6
succinate + 8-methylmenaquinone-6
-
-
-
-
?
fumarate + a menaquinol
succinate + a menaquinone
-
the enzyme is involved in anaerobic metabolism
-
-
?
fumarate + a quinol
succinate + a quinone
fumarate + anthrahydroquinonesulfonate
succinate + anthraquinonesulfonate
fumarate + electron donor
succinate + oxidized donor
fumarate + menaquinol
succinate + ?
fumarate + menaquinol
succinate + menaquinone
fumarate + menaquinol-6
succinate + menaquinone-6
-
-
-
-
r
fumarate + naphthoquinol
succinate + naphthoquinone
-
-
-
-
r
fumarate + quinol
succinate + ubiquinone
fumarate + reduced 2,6-dichlorophenolindophenol
succinate + 2,6-dichlorophenolindophenol
-
-
-
-
r
fumarate + reduced acceptor
succinate + acceptor
fumarate + reduced benzyl viologen
succinate + benzyl viologen
fumarate + reduced benzyl viologen
succinate + oxidized benzyl viologen
-
-
-
r
fumarate + reduced decylubiquinone
succinate + decylubiquinone
-
-
-
-
r
fumarate + reduced phenazine methosulfate
succinate + phenazine methosulfate
-
enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities
-
-
r
fumarate + reduced plumbagin
succinate + oxidized plumbagin
-
-
-
-
?
succinate + 1,4-naphthoquinone
fumarate + 1,4-naphthoquinol
succinate + 1-methoxy-5-methylphenazinium methyl sulfate
fumarate + ?
-
-
-
-
?
succinate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinol
-
the redox potential of the 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinone/2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinol couple is 90 mV higher than that of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple
-
-
?
succinate + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-1,4-benzohydroquinone
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinol
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
succinate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol
-
-
-
-
r
succinate + 2,3-dimethyl-1,4-naphthoquinone
fumarate + 2,3-dimethyl-1,4-naphthoquinol
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
r
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
succinate + 2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
?
-
i.e. MTT, in presence of phenazine methosulfate, i.e. PMS
-
-
?
succinate + 2-ethyl-3-methyl-1,4-naphthoquinone
fumarate + 2-ethyl-3-methyl-1,4-naphthoquinol
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
?
succinate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone
fumarate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol
-
the succinate dehydrogenase C subunit is responsible for ubiquinone binding
-
?
succinate + a menaquinone
fumarate + a menaquinol
succinate + a quinone
fumarate + a quinol
succinate + acceptor
fumarate + reduced acceptor
succinate + benzyl viologen
fumarate + reduced benzyl viologen
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
succinate + decylubiquinone
fumarate + ?
-
-
-
-
?
succinate + decylubiquinone
fumarate + decylubiquinol
succinate + decylubiquinone
fumarate + reduced decylubiquinone
-
-
-
-
r
succinate + duroquinone
fumarate + duroquinol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
succinate + FAD
fumarate + FADH2
succinate + ferricyanide
fumarate + ferrocyanide
succinate + ferrocyanide
fumarate + ferricyanide
succinate + menadione
fumarate + menadiol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + menaquinone
fumarate + menaquinol
succinate + methylene blue
?
-
-
-
-
?
succinate + nitro blue tetrazolium
fumarate + formazan
-
yellow dye
blue dye
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
succinate + oxidized benzyl viologen
fumarate + reduced benzyl viologen
-
-
-
r
succinate + oxidized donor
?
-
endogenous SDH activity results in blue diphormazan deposits from the nitroblue tetrazolium reduction through succinate oxidation
-
-
?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
succinate + oxidized phenazine ethosulfate
fumarate + reduced phenazine ethosulfate
-
-
-
-
r
succinate + oxidized phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
?
succinate + phenazine ethosulfate
fumarate + reduced phenazine ethosulfate
-
-
-
-
?
succinate + phenazine methosulfate
fumarate + ?
-
phenazine methosulfate as direct electron acceptor and 2,6-dichlorophenolindophenol as final acceptor
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
succinate + phenazine methosulfate + 2,6-dichlorophenolindophenol
fumarate + ?
-
quinone reduction by Rhodothermus marinus succinate:menaquinone oxidoreductase is not stimulated by the membrane potential
-
-
?
succinate + rhodoquinone
fumarate + rhodoquinol
succinate + ubiquinone
fumarate + ubiquinol
succinate + ubiquinone-1
fumarate + ubiquinol
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
-
-
r
succinate + ubiquinone-1
fumarate + ubiquinol-1
succinate + ubiquinone-2
fumarate + ubiquinol
succinate + ubiquinone-8
fumarate + ubiquinol-8
-
-
-
r
succinate + WST-1
fumarate + reduced WST-1
-
-
-
-
?
ubiquinone-1 + L-malate
?
ubiquinone-1 + succinate
ubiquinol + fumarate
ubiquinone-1 + succinate
ubiquinol-1 + fumarate
additional information
?
-
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
mutation of His-82 to Arg in fumarate reductase subunit C prevents oxidation of 2,3-dimethyl-1,4-naphthohydroquinone
-
r
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
-
-
?
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
-
-
?
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
reaction catalyzed by fumarate reductase complex, the site of the complex reacting with fumarate is situated on the 79000 Da subunit, and the site reacting with dimethylnaphthohydroquinone is cytochrome b
-
?, r
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
cytochrome b-dependent in both directions
-
r
fumarate + a quinol
succinate + a quinone
-
-
-
r
fumarate + a quinol
succinate + a quinone
-
-
-
r
fumarate + anthrahydroquinonesulfonate
succinate + anthraquinonesulfonate
-
-
-
?
fumarate + anthrahydroquinonesulfonate
succinate + anthraquinonesulfonate
-
reaction catalyzed in the presence or absence of cytochrome b
-
?
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
?
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
-
donor: benzyl viologen
-
-
?
fumarate + electron donor
succinate + oxidized donor
-
main reaction for fumarate reductase, reverse reaction only 1% of fumarate reduction
-
-
?
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
?
fumarate + electron donor
succinate + oxidized donor
-
donor: anthrahydroquinonesulfonate
-
-
r
fumarate + menaquinol
succinate + ?
-
-
-
?
fumarate + menaquinol
succinate + ?
-
-
-
?
fumarate + menaquinol
succinate + menaquinone
-
-
-
-
r
fumarate + menaquinol
succinate + menaquinone
-
-
-
-
r
fumarate + menaquinol
succinate + menaquinone
-
-
-
r
fumarate + menaquinol
succinate + menaquinone
-
-
-
?
fumarate + menaquinol
succinate + menaquinone
-
fumarate reductase acts as part of an anaerobic respiratory chain
-
-
r
fumarate + menaquinol
succinate + menaquinone
enzyme is expressed under anaerobic conditions, transcription is coupled to that of the succinate-ubiquinone oxidase, EC 1.3.5.1
-
-
r
fumarate + menaquinol
succinate + menaquinone
-
the enzyme catalyzes the terminal step of the phosphorylative electron transport
-
?
fumarate + menaquinol
succinate + menaquinone
-
the enzyme catalyzes the terminal step of the phosphorylative electron transport
-
?
fumarate + quinol
succinate + ubiquinone
-
-
-
r
fumarate + quinol
succinate + ubiquinone
-
-
-
r
fumarate + quinol
succinate + ubiquinone
-
-
-
r
fumarate + reduced acceptor
succinate + acceptor
the obligate autotroph requires fumarate reductase activity if it performs CO2 fixation via a reductive citric acid cycle
-
-
r
fumarate + reduced acceptor
succinate + acceptor
-
FrdCAB functions in vivo as both the fumarate reductase and the succinate dehydrogenase, with an apparent energetic cost when catalyzing succinate oxidation
-
-
r
fumarate + reduced benzyl viologen
succinate + benzyl viologen
-
-
-
-
r
fumarate + reduced benzyl viologen
succinate + benzyl viologen
-
-
-
-
?
fumarate + reduced benzyl viologen
succinate + benzyl viologen
-
-
-
-
?
fumarate + reduced benzyl viologen
succinate + benzyl viologen
-
-
-
-
?
succinate + 1,4-naphthoquinone
fumarate + 1,4-naphthoquinol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + 1,4-naphthoquinone
fumarate + 1,4-naphthoquinol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
-
-
-
-
r
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
-
-
-
-
?
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
ir
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
ir
succinate + a menaquinone
fumarate + a menaquinol
-
-
-
-
?
succinate + a menaquinone
fumarate + a menaquinol
-
the enzyme is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
-
?
succinate + a quinone
fumarate + a quinol
-
-
-
r
succinate + a quinone
fumarate + a quinol
-
-
-
r
succinate + acceptor
fumarate + reduced acceptor
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
Sdh produces only superoxide and no H2O2 upon flavin autoxidation, even at high concentrations of succinate
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
caldariellaquinone, the physiologically acting electron mediator in Sulfolobus membranes is slowly reduced as compared to water-soluble dyes
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
caldariellaquinone, the physiologically acting electron mediator in Sulfolobus membranes is slowly reduced as compared to water-soluble dyes
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + decylubiquinone
fumarate + decylubiquinol
-
-
-
-
?
succinate + decylubiquinone
fumarate + decylubiquinol
-
-
-
-
?
succinate + decylubiquinone
fumarate + decylubiquinol
-
decylubiquinone-mediated reduction of dichlorophenol indophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: dichloroindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
active in aerobic respiration, repressed during anaerobic respiration
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: phenazine methosulfate and 2,6-dichloroindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
comparison of assay methods
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: phenazine methosulfate and 2,6-dichloroindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: methylene blue (oxidized)
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
r
succinate + FAD
fumarate + FADH2
-
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
?
succinate + FAD
fumarate + FADH2
-
-
-
?
succinate + ferricyanide
fumarate + ferrocyanide
-
-
-
-
r
succinate + ferricyanide
fumarate + ferrocyanide
-
-
-
-
r
succinate + ferricyanide
fumarate + ferrocyanide
-
-
-
?
succinate + ferricyanide
fumarate + ferrocyanide
-
the assay is based on the reduction of ferricyanide to ferrocyanide by SDH activity and on the coupled capture of ferrocyanide by copper. The granular reaction product (copperferrocyanide) is highly electron opaque and is confined exclusively to the mitochondrial membranes.The use of a chelating agent in the incubating medium prevents the diffusion of the dark spots and guarantees their precise localization at the site of SDH activity
-
-
?
succinate + ferrocyanide
fumarate + ferricyanide
-
-
-
?
succinate + ferrocyanide
fumarate + ferricyanide
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
-
-
-
-
r
succinate + menaquinone
fumarate + menaquinol
-
-
-
-
r
succinate + menaquinone
fumarate + menaquinol
-
-
-
-
r
succinate + menaquinone
fumarate + menaquinol
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
-
-
-
r
succinate + menaquinone
fumarate + menaquinol
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
QFR can also catalyze the reverse reaction, succinate oxidation, albeit with slower kinetics and poorer catalytic efficiency
-
-
r
succinate + menaquinone
fumarate + menaquinol
Megalodesulfovibrio gigas
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
Megalodesulfovibrio gigas DSM 1382
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
-
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
-
-
-
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
-
in the presence of the artificial electron acceptor phenazine methosulfate and the ubiquinone analogue UQ1
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
-
in presence of phenazine methosulfate
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
-
-
-
-
r
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
-
-
-
-
r
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
r
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
in presence of phenazine methosulfate
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
succinate-dependent, phenazine methosulfate-mediated malonate-sensitive reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
-
-
-
?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
-
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
with 2,6-dichlorophenolindophenol, best substrate
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
with 2,6-dichlorophenolindophenol, best substrate
-
-
?
succinate + rhodoquinone
fumarate + rhodoquinol
-
-
-
?
succinate + rhodoquinone
fumarate + rhodoquinol
rhodoquinone binding site, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
the succinate dehydrogenase activity of mitochondria in adults and larvae are comparable
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
electron acceptor: menaquinone
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
slow inactivation of the the enzyme in the substrate assay mixture containing different concentrations of substrates, succinate and 2,6-dichloroindophenol, the inactivation rate decreases with increasing concentration of succinate, the inactivation is 2,6-dichloroindophenol concentration independent
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
succinate dehydrogenase restores full activity to electron transport particles or complex II preparations whose succinate dehydrogenases have been selectively destroyed at pH 9.3
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
complex II of the mitochondrial oxidative phosphorylating system
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
complex II is the only membrane bound enzyme of the Krebs cycle, and it feeds electrons into the electron transport chain from the oxidation of succinate
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
electrons move from the FAD prosthetic group in SDH on to the two matrix subunits via a series of [Fe-S] redox clusters and possibly also via a heme group to end up at the terminal acceptor ubiquinone residing within the membrane subunits CybL and CybS
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
succinate dehydrogenase is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
the enzyme does not generate a proton motive force during catalysis and are electroneutral, thus, the quinone reduction reaction must consume cytoplasmic protons which are released stoichiometrically during succinate oxidation. Residues SdhBG227, SdhCD95, and SdhCE101 are located at or near the entrance of a water channel that functions as a proton wire connecting the cytoplasm to the quinone binding site in vivo, while an alternative proton pathway exists in vitro only, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
SDH is a key enzyme that catalyses the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Functioning as mitochondrial complex II in the electron transport chain, it transfers electrons extracted from succinate to ubiquinone
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
the enzyme is part of the tricarboxylic acid cycle, it is also a tumor suppressor. Succinate stabilizes and activates hypoxia-inducible factor HIFalpha and reversibly and competitively inhibits HIF-prolyl hydroxylase leading to induction of hypoxia in SDH-deficient cells, 2-oxoglutarate overcomes succinate-mediated inhibition of PHD in vitro, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
determination of quinol:fumarate reductase activity using 2,3-dimethyl-1,4-naphthoquinol
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol, role of Tyr-89 in the protonation of ubiquinone
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
SDH is an essential component of the electron transport chain and of the tricarboxylic acid cycle in the mitochondrial membrane
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
a key membrane complex in the tricarboxylic acid cycle that catalyzes the oxidation of succinate to fumarate in the mitochondrial matrix as succinate dehydrogenase
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
electrons are transferred from succinate to ubiquinone through the buried prosthetic groups FAD, [2Fe-2S] cluster, [4Fe-4S] cluster [3Fe-4S] cluster and heme, which form an integral part of the complex
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
succinate + ubiquinone-1
fumarate + ubiquinol-1
-
-
-
-
?
succinate + ubiquinone-1
fumarate + ubiquinol-1
-
-
-
-
?
succinate + ubiquinone-2
fumarate + ubiquinol
-
-
-
-
r
succinate + ubiquinone-2
fumarate + ubiquinol
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
-
-
r
ubiquinone-1 + L-malate
?
-
-
-
-
?
ubiquinone-1 + L-malate
?
-
-
-
-
?
ubiquinone-1 + L-malate
?
-
-
-
-
?
ubiquinone-1 + L-malate
?
-
-
-
-
?
ubiquinone-1 + L-malate
?
-
-
-
-
?
ubiquinone-1 + L-malate
?
-
-
-
-
?
ubiquinone-1 + L-malate
?
-
-
-
-
?
ubiquinone-1 + succinate
ubiquinol + fumarate
-
-
-
-
?
ubiquinone-1 + succinate
ubiquinol + fumarate
-
-
-
-
?
ubiquinone-1 + succinate
ubiquinol-1 + fumarate
-
-
-
-
?
ubiquinone-1 + succinate
ubiquinol-1 + fumarate
-
-
-
-
?
ubiquinone-1 + succinate
ubiquinol-1 + fumarate
-
-
-
-
?
ubiquinone-1 + succinate
ubiquinol-1 + fumarate
-
-
-
-
?
additional information
?
-
-
fumarate reductase activity of larval complex II is less than 3% of that of adult enzyme, complex II of adult nematode functions in the reverse direction as a fumarate reductase rather than as a succinate dehydrogenase
-
-
?
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
-
complex II of adult organism muscle exhibits high fumarate reductase activity and plays a key role in anaerobic electron-transport during adaptation to their microaerobic habitat, in contrast larval complex II shows a much lower fumarate reductase activity than the adult enzyme and functions as succinate dehydrogenase in aerobic respiration
-
-
?
additional information
?
-
-
complex II from mitochondria of the adult parasitic nematode exhibits a high fumarate reductase activity and plays a key role in the anaerobic electron transport observed in these organelles
-
-
?
additional information
?
-
-
enzyme also accepts reduced decylubiquinone, reaction of EC 1.3.5.1
-
-
?
additional information
?
-
-
enzyme also accetps phenazine methosulfate, reaction of EC 1.3.5.4
-
-
?
additional information
?
-
-
evidence for proton potential dependent catalysis of succinate oxidation by quinone as well as for proton potential generation upon catalysis of fumarate reduction by quinol
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
-
pathway of electron transfer in complex II
-
-
?
additional information
?
-
-
the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
-
-
?
additional information
?
-
-
electronic communication between purified SQR and a surface modified gold capillary electrode, redox titrations, overview
-
-
?
additional information
?
-
-
electronic communication between purified SQR and a surface modified gold capillary electrode, redox titrations, overview
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
reduction of coenzyme Q and analogues, coenzyme Q2 is the most efficient electron acceptor, coenzyme Q10 in substrate quantities when supplemented with Triton X-100 and a lipid extract is about 75% as efficient as coenzyme Q2
-
-
?
additional information
?
-
-
L- or D-malate oxidation
-
-
?
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
-
study of potential dependecy and pH dependency of reaction, tunnel-diopde effect
-
-
?
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
?
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
?
additional information
?
-
-
vitamin E analogues bind to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
-
-
?
additional information
?
-
for enzymatic activity the succinate-dependent, phenazine methosulfate-mediated reduction of dichlorophenol indophenol of crude mitochondrial fractions prepared from the wild type and the P211 mutants is measured
-
-
?
additional information
?
-
-
for enzymatic activity the succinate-dependent, phenazine methosulfate-mediated reduction of dichlorophenol indophenol of crude mitochondrial fractions prepared from the wild type and the P211 mutants is measured
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
efficiency with different quinones, in decreasing order: phenazine methosulfate, decylubiquinone, duroquinone, menadione, 2,3-dimethyl-1,4-naphthoquinone
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
-
pathway of electron transfer in complex II
-
-
?
additional information
?
-
-
study of potential dependecy and pH dependency of reaction, tunnel-diopde effect
-
-
?
additional information
?
-
-
model of fumarate reductase electron-transport chain
-
-
?
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
?
additional information
?
-
-
enzyme also accepts artificial electron acceptors, reaction of EC 1.3.99.1
-
-
?
additional information
?
-
-
enzyme operates with both natural quinones, ubiquinone and menaquinone, at a single quinone binding site. Residue Lys228 in subunit FrdB provides a strong hydrogen bond to menaquinone and is essential for reactions with both quinone types. There is similar hydrogen bonding of the C1 carbonyl of both MQ and UQ, whereas there is different hydrogen bonding for their C4 carbonyls
-
-
?
additional information
?
-
-
dichlorophenolindophenol only acceptor when used together with phenazine methosulfate, no reaction with ubiquinones, see EC 1.3.5.1 for SDH- and FRD-complex
-
-
?
additional information
?
-
-
approximately 10% to 15% of paragangliomas are caused by mutations in the succinate dehydrogenase genes SDHB, SDHC, or SDHD
-
-
?
additional information
?
-
-
enzyme subunit mutations are involved in the Carney-Stratakis syndrome and in development of gastrointestinal stromal tumors, overview
-
-
?
additional information
?
-
-
germline mutations in the SDHB, SDHC or SDHD genes cause hereditary paraganglioma tumors which show constitutive activation of homeostatic mechanisms induced by oxygen deprivation/hypoxia, overview
-
-
?
additional information
?
-
-
germline mutations of the gene SDHB encoding succinate dehydrogenase subunit B predispose to malignant paraganglioma. Despite an autosomal dominant pattern of inheritance, penetrance of the disease is incomplete and age dependent, overview
-
-
?
additional information
?
-
-
germline mutations of the SDHB gene are correlated to an elevated risk of malignant, extradrenal tumor development, overview
-
-
?
additional information
?
-
-
high frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain, mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations
-
-
?
additional information
?
-
-
inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: implications for the pathogenesis and treatment of mitochondrial encephalomyopathies, overview
-
-
?
additional information
?
-
-
mitochondrial dysfunction by complex II inhibition delays overall cell cycle progression via reactive oxygen species production, overview, complex II defects are involved in ageing and cancers such as hereditary paraganglioma and familial pheochromocytoma, overview
-
-
?
additional information
?
-
-
mutations of the enzyme can cause hereditary paraganglioma and/or pheochromocytoma, overview
-
-
?
additional information
?
-
-
subunit mutations are involved in development of malignant paragangliomas
-
-
?
additional information
?
-
-
succinate dehydrogenase enzyme subunit B gene mutations cause metastatic pheochromocytoma and paraganglioma, distribution of metastases in different tissues in correlation to the enzyme expression, sites of bone involvement, overview
-
-
?
additional information
?
-
-
the Cowden or Cowden-like syndromes are caused by PTEN mutations of the SDH-D gene, encoding the subunit D, the syndromes are associated with breast, thyroid and endometrial neoplasias, overview
-
-
?
additional information
?
-
-
the nuclear genes SDHD and SDHB encode two mitochondrial enzyme complex II subunits and are associated with the development of familial pheochromocytomas and paraganglioma, i.e. the hereditary pheochromocytoma/paraganglioma syndrome, HPPS, and the following metastasis, overview
-
-
?
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
analysis of the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas, overview
-
-
-
additional information
?
-
Megalodesulfovibrio gigas DSM 1382
analysis of the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas, overview
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
-
-
?
additional information
?
-
-
membrane-bound enzyme of the citric acid cycle and the respiratory chain
-
-
?
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
-
enzyme assay using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide method
-
-
?
additional information
?
-
the flavoprotein of succinate dehydrogenase is an in vitro substrate of and phosphorylated at Tyr535 and Tyr596 by the Fgr tyrosine kinase, overview
-
-
?
additional information
?
-
determination of the activity of succinate dehydrogenase by 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyl-tetrazolium bromide reduction and by reduction of electron acceptor dichlorophenolindophenol (DCPIP)
-
-
-
additional information
?
-
determination of the activity of succinate dehydrogenase by 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyl-tetrazolium bromide reduction and by reduction of electron acceptor dichlorophenolindophenol (DCPIP)
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
?
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
?
additional information
?
-
-
succinate dehydrogenase flavoprotein subunit Sdh1p is bound by the mitochondrial FAD transporter, Flx1p, a member of the mitochondrial carrier family responsible for FAD transport in Saccharomyces cerevisiae, FLX1p controls SDH activity by regulating the amount of flavinylated Sdh1p, overview
-
-
?
additional information
?
-
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
?
additional information
?
-
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
?
additional information
?
-
-
catalytic mechanism
-
-
?
additional information
?
-
-
no activity with 1,4-benzoquinone
-
-
?
additional information
?
-
-
no activity with 1,4-benzoquinone
-
-
?
additional information
?
-
-
pathway of electron transfer in complex II
-
-
?
additional information
?
-
-
the fumarate reductase complex has two different reactive sites, which are essential for its function in the phosphorylative electron transport of the bacterium
-
-
?
additional information
?
-
-
succinate dehydrogenase is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain, fumarate reductase participates in anaerobic respiration with fumarate as the terminal electron acceptor and is part of the electron transport chain catalysing the oxidation of various donor substrates by fumarate
-
-
?
additional information
?
-
-
fumarate reduction activity is measured by monitoring photometrically the oxidation of dithionite-reduced benzylviologen by fumarate
-
-
?
additional information
?
-
-
succinate oxidation activity is determined using either methylene blue, dichlorophenolindophenol, ferricenium hexafluorophosphate, dimethylnaphthoquinone or as electron acceptor. Strikingly, no succinate oxidation activity is be detected, independent of the electron acceptor
-
-
?
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1-methoxy-5-methylphenazinium methyl sulfate
-
-
2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
-
-
2,6-dichlorophenolindophenol
flavin adenine dinucleotide
heme b556
-
ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
heme b562
-
the enzyme has a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
menaquinone
Megalodesulfovibrio gigas
one menaquinone molecule is bound near heme bL in the hydrophobic subunit C
Plumbagin
-
a quinone analogue
quinone
-
with a periplasmically oriented quinone binding site of the enzyme
[3Fe-4S]-center
located in subunit FrdC
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
in presence of phenazine methosulfate
cytochrome b
-
-
-
cytochrome b
-
2 mol per mol FAD
-
cytochrome b
-
cytochrome b-558, 3.6 nmol per mg of protein, functions as electron carrier between NADH dehydrogenase and succinate dehydrogenase in the Ascaris NADH-fumarate reductase system
-
cytochrome b
-
2 mol per mol of FAD
-
cytochrome b
-
cytochrome b-558, is the smallest protein of the complex with MW: 19000, it is a transmembrane protein and anchors succinate dehydrogenase to the cytoplasmic side of the membrane
-
cytochrome b
-
fumarate reductase contains a diheme cytochrome b
-
cytochrome b
-
4.5-5 nmol cytochrome b per mg protein
-
cytochrome b
-
has a MW of 25000 Da, a midpoint potential of - 15 mV and is reducible by dimethylnaphthohydroquinone in the absence of the other subunits
-
cytochrome b
-
succinate dehydrogenase contains one heme b
-
cytochrome b
-
the enzyme contains a cytochrome b with a midpoint potential of -20 mV, referred to as the high-potential cytochrome b and a cytochrome b with a midpoint potential of -200 mV, referred to as the low-potential cytochrome b
-
cytochrome b
-
the isolated two-subunit membrane anchoring protein contains 35 nmol cytochrome b-556 per mg protein
-
cytochrome b
-
cytochrome b-557.5
-
cytochrome b
-
cytochrome b-558, composed of two hydrophobic polypeptides with molecular masses of 17.2 and 12.5 kDa, which correspond to the two small subunits of complex II
-
cytochrome b
-
1 mol per mol of succinate dehydrogenase
-
cytochrome b-560
-
-
-
FAD
-
-
FAD
-
covalently bound to flavoprotein subunit
FAD
-
covalently bound to flavoprotein subunit
FAD
-
covalently bound to flavoprotein subunit
FAD
-
covalently bound to flavoprotein subunit
FAD
-
one protein-bound FAD linked to the 79000 Da peptide
FAD
-
1 mol of covalently bound flavin per 100,000 g of protein
FAD
-
role in succinate oxidation
FAD
-
1 mol flavin per mol succinate dehydrogenase
FAD
-
covalently linked to larger subunit
FAD
-
amino acid sequence around FAD-binding site
FAD
-
covalently bound to FRDA subunit
FAD
-
covalently linked to protein histidyl residue
FAD
-
flavoprotein subunit SdhA
FAD
-
localized in Sdh1, i.e. the flavoprotein subunit
FAD
-
covalent FAD modification of flavoprotein subunit 1 from complex II
FAD
-
ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
FAD
-
flavoprotein, 41 pmol FAD per mg of protein in wild-type strain YPH499, possesses a flavoprotein subunit Sdh1p as part of the catalytic dimer of the tetrameric enzyme
FAD
-
FAD is non-covalently attached to SdhA. The reason for the lack of succinate oxidation activity might be explained by the absence of a covalently bound FAD which seems to be a prerequisite for succinate oxidation activity
FAD
-
proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
FAD
-
proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
FAD
covalently attached to the enzyme to enable succinate oxidation
FAD
-
non-covalenly bound. In the enzyme containing a mutant A86H flavoprotein subunit the FAD is covalently bound
FAD
-
prosthetic group of fumarate reductase is covalently bound FAD. The specific activity of fumarate reductase is increased to the same extent as the content of the covalently bound FAD when the membrane is fractionated with cholate and ammonium sulfate. The acid-extractable FAD is removed by this procedure
FAD
-
stoichiometric ratio between covalently bound FAD and the iron-sulfur cluster is 1:1. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD
FAD
-
subunit A comprises a large FAD-binding domain
FAD
-
bound in the succinate dehydrogenase flavoprotein, SdhA, subunit
FAD
-
bound in the succinate dehydrogenase flavoprotein, SdhA, subunit
FAD
-
FAD of Sdh1 is covalently attached at an active site His residue, 8alpha-N3-histidyl-FAD linkage, involving Arg582, required for enzyme activity. Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit. FAD binding is important to stabilize the Sdh1 conformation enabling association with Sdh2 and the membrane anchor subunits
FAD
-
flavinylation of SDH is dependent on SDH1:SDHA F2 interaction requiring the C-terminal tail of SDH1
FAD
SdhA is the FAD-containing subunit
FAD
the enzyme complex contains one molecule of covalently bound FAD
FAD
the FAD prosthetic group is held in the FAD binding domain by a covalent bond to His A79 and by hydrogen bonds with highly conserved residues, overview
FAD
bound in the SdhA subunit
FAD
bound in the SdhA subunit
FAD
bound to flavoprotein FrdA
FAD
bound to the binding site for FAD in the FAD-binding domain (residues 1-245 and 351-431), which includes a Rossmann-type fold
FAD
covalently attached FAD within the FrdA subunit, the SdhE assembly factor enhances covalent flavinylation of complex II homologues. Analysis of the mechanisms of covalent flavinylation of FrdA subunit, and propose of chemical mechanism of covalent flavinylation via a quinone-methide intermediate, overview. In Escherichia coli QFR, the flavin is covalently attached to the FrdA subunit via an 8x02 linkage to the N-epsilon of His44. This places the flavin isoalloxazine group at the interface of two domains, termed the flavin-binding domain and the capping domain. These domains can move with respect to each other, which may allow the catalytic subunit to close over the substrate-bound active site and protect the reaction intermediates from solvent. Quantitation of covalent flavinylation under aerobic and anaerobic growth conditions
FAD
covalently bound in the SDHA subunit, for electrons travel from FAD in SDHA, via three Fe-S clusters in SDHB, to the quinone-binding site at the membrane interface. Significance of FAD covalent bond versus non-covalent bond. FAD is mandatory for enzyme activity. In yeast, a soluble, mitochondrial matrix protein named Sdh5 is required for the activation and flavination of Sdh1 (SDH flavoprotein subunit homologue) as well as for SDH-dependent respiration
FAD
covalently bound in the SDHA subunit, for electrons travel from FAD in SDHA, via three Fe-S clusters in SDHB, to the quinone-binding site at the membrane interface. Significance of FAD covalent bond versus non-covalent bond. FAD is mandatory for enzyme activity. Under aerobic conditions, the FAD moiety catalyzes succinate oxidation, upon which FAD is itself reduced to FADH2. Changes in redox potential prompt electrons to move from the reduced FADH2 through Fe-S clusters in SdhB to eventually reduce ubiquinone at the ubiquinone-binding site formed by SdhC and SdhD
Fe-S center
-
the Fe-S centers in Sdh2 consist of a 2Fe-2S center proximal to the FAD site, an adjacent 4Fe-4S center followed by a 3Fe-4S center
Fe-S center
iron-sulfur protein FrdB
Fe-S cluster
-
Fe-S cluster
SDHB is an iron-sulfur cluster protein containing three Fe-S clusters
Fe-S cluster
SDHB is an iron-sulfur cluster protein containing three Fe-S clusters
Fe-S cluster
the SDHB subunit of the enzyme complex contains three iron-sulfur clusters (ISCs): [2Fe-2S], [4Fe-4S], and [3Fe-4S]
Fe-S cluster
the SDHB subunit of the enzyme complex contains three iron-sulfur clusters (ISCs): [2Fe-2S], [4Fe-4S], and [3Fe-4S]
Fe-S cluster
three clusters
flavin
-
-
flavin
flavoprotein of succinate dehydrogenase
flavin
-
quantitative determination of content in wild-type and mutant enzymes
flavin
-
covalently-bound flavin cofactor
flavin
the enzyme complex contains non-extractable flavin. The purified complex contains 4.6 nmol/mg acid non-extractable flavin
flavin adenine dinucleotide
-
-
flavin adenine dinucleotide
-
-
heme
-
-
heme
-
single heme localized between Sdh3 and Sdh4 subunits
heme
-
direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
heme
-
a single heme b moiety is incorporated into the membrane anchor and only the QP-site is functional
heme
-
in a di-heme membrane anchor protein harboring two putative quinone binding sites
heme
-
the residues required for heme-binding are harbored by SdhC
heme
-
proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
heme
-
proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
heme
-
enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD
heme
-
enzyme contains two heme molecules. Presence of protoheme IX, absence of the other heme types. The ratio of protoheme IX to the SQR protomer is 1.5, there are two protoheme IX-binding sites in SQR
heme
-
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
heme
-
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
heme
-
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
heme
-
the enzyme contains two heme b cofactors, a di-heme
heme
SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them
heme
SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them
heme b
-
-
heme b
-
heme bP und heme bD
heme b
-
the quinone binding site of succinate dehydrogenase is required for electron transfer to the heme b
heme b
-
the enzyme contains one hydrophobic subunit (C) with two haem b groups
heme b
-
the enzyme contains one hydrophobic subunit (menaquinol-oxidising subunit C) with two haem b groups. The binding of the two heme molecules is described. The close proximity between the two hemes offers a straightforward possibility for transmembrane electron transfer
heme b
Megalodesulfovibrio gigas
two b-hemes are bound per homodimer
iron-sulfur centre
-
direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
iron-sulfur centre
-
ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
iron-sulfur centre
-
enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes. The purified mQFR complex has two iron-sulfur centers of the ferredoxin type that are paramagnetic in the reduced state, 2Fe-2S and 4Fe-4S, and one iron-sulfur center of the high potential type that is paramagnetic in the oxidized state, 3Fe-4S. Centers 2Fe-2S and 4Fe-4S exhibit a large difference in their redox midpoint potential, center 2Fe-2S is reducible with succinate, whereas the latter one can only be reduced by very low potential reductant such as dithionite
iron-sulfur centre
-
enzyme contains the canonical iron-sulfur centers S1, S2, and S3, as well as two B-type hemes. The S3 center has a high reduction potential of +130 mV and is present in two different conformations, one of which presents an EPR signal with g values at 2.035, 2.009, and 2.001. The apparent midpoint reduction potentials of the hemes, +75 and -65 mV at pH 7.5, are higher than those reported for other enzymes. The heme with the lower potential, heme bL, presents a considerable dependence of the reduction potential with pH, i.e. a redox-Bohr effect, having a pKox of 6.5 and a pKred of 8.7. This behavior is consistent with the proposal that in these enzymes menaquinone reduction occurs close to heme bL, near to the periplasmic side of the membrane, and involving dissipation of the proton transmembrane gradient
iron-sulfur centre
-
the iron-sulfur protein of the electron transport phosphorylation system is the donor for fumarate reductase
iron-sulfur centre
-
SdhB
phenazine methosulfate
-
-
phenazine methosulfate
-
-
ubiquinone
-
-
ubiquinone
-
the residues required for quinone-binding are harbored by SdhD
ubiquinone
-
two putative binding sites in the di-heme membrane anchoring protein
additional information
-
analysis of the functional role of the trinuclear cluster S3 in the enzyme by introducing a fourth cysteine residue into the putative ligation motif to that cluster
-
additional information
-
measurement of the redox potentials of the sulfur-centers
-
additional information
-
measurement of the redox potentials of the sulfur-centers
-
additional information
-
measurement of the redox potentials of the sulfur-centers
-
additional information
-
measurement of the redox potentials of the sulfur-centers
-
additional information
-
the enzyme contains acid-labile sulfides
-
additional information
-
the fumarate reductase of the parasitic adult and the succinate dehydrogenase of free-living larvae share a common iron-sulfur subunit, at least the flavoprotein subunit and the small subunit of cytochrome b of the larval complex II differ from those of adult
-
additional information
-
the enzyme contains 18-20% lipid by weight protein
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
preparations of complex II contain 0.2 mg lipid per mg protein and 7-8 mol of acid-labile sulfide per 100,000 g of protein
-
additional information
-
the iron-sulfur clusters are located in one or both of the hydrophilic subunits, centre 2 in fumarate reductase is a 4Fe-4S cluster
-
additional information
-
two hydrophobic subunits (C and D) which bind either no haem b group
-
additional information
-
two hydrophobic subunits (C and D) which bind either one haem b group
-
additional information
-
SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
-
additional information
the enzyme structure comprises four subunits and five co-factors, cofactor structure comparisons, overview
-
additional information
-
the enzyme structure comprises four subunits and five co-factors, cofactor structure comparisons, overview
-
additional information
the biogenesis of flavinylated SdhA, the catalytic subunit of SQR, is assisted by a highly conserved assembly factor termed SdhE in bacteria via an unknown mechanism. SdhE makes a direct interaction with the flavin adenine dinucleotide-linked residue His45 in SdhA and maintains the capping domain of SdhA in an open conformation. This displaces the catalytic residues of the succinate dehydrogenase active site by as much as 9.0 A compared with SdhA in the assembled SQR complex. These data suggest that bacterial SdhE proteins, and their mitochondrial homologues, are assembly chaperones that constrain the conformation of SdhA to facilitate efficient flavinylation while regulating succinate dehydrogenase activity for productive biogenesis of SQR. The SdhE protein forms an intimate complex with SdhA, with a buried surface area. Three regions of SdhE make contact with the SdhA protein, namely residues 5-25 (which encompass helix alpha1, the N terminus of alpha2, and the loop that connects these two regions), residues 47-61 (which form helix alpha4), and residues 80-86 (which form the C-terminus). Binding structure, detailed overview. rotation of the SdhA capping domain accompanies formation of the SdhAE complex. SdhE stabilizes SdhA in a nonactive conformation during assembly, mechanism of action of SdhE in the biogenesis of holo-SdhA
-
additional information
the SdhE assembly factor binds directly to the FrdA subunit prior to assembly into the intact complex. The interaction involves a surface of SdhE containing a conserved RGXXE motif. SdhE is required for enzyme complex function, it promotes covalent flavinylation of FrdA subunit
-
additional information
-
the SdhE assembly factor binds directly to the FrdA subunit prior to assembly into the intact complex. The interaction involves a surface of SdhE containing a conserved RGXXE motif. SdhE is required for enzyme complex function, it promotes covalent flavinylation of FrdA subunit
-
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(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
2-alkyl-4,6-dinitrophenol-17
-
-
2-alkyl-4,6-dinitrophenol-20
-
-
2-alkyl-4,6-dinitrophenols
2-bromo-3-ethyl-1,4-naphthoquinone
-
2-bromo-3-methyl-1,4-naphthoquinone
-
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
2-heptyl-4-hydroxyquinoline N-oxide
2-n-heptyl-4 hydroxyquinoline N-oxide
-
a specific inhibitor, i.e. HQNO, which binds to quinone binding site Qd in SQR
2-n-heptyl-4-hydroxyquinoline
-
inhibition of succinate dehydrogenase activity using 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone or 2,6-dichlorophenolindophenol as electron acceptor
2-n-heptyl-4-hydroxyquinoline N-oxide
-
inhibitory to the succinate dehydrogenase activity assay using 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone and 2,6-dichloroindophenol as the electron acceptor, not inhibitory to the succinate dehydrogenase activity assay using phenazine methosulfate and 2,6-dichloroindophenol
2-n-heptyl-4-hydroxyquinoline-N-oxide
2-n-heptyl-4-hydroxyquinolino-N-oxide
-
-
2-sec-butyl-4,6-dinitrophenol
-
non-competitive inhibition
2-thenoyltrifluoracetone
-
EC50 fumarate reductase 0.026 mM, EC50 succinate dehydrogenase 0.028 mM
2-Thenoyltrifluoroacetone
2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
3-(difluoromethyl)-1-methyl-N-(1-[(2-bromophenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
-
compound exhibits good preventive effects against Rhizoctonia solani
3-(difluoromethyl)-1-methyl-N-(1-[(3,5-dimethylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
-
noncompetitive inhibition with respect to cytochrome c and 2,6-dichlorophenol indophenol
3-(difluoromethyl)-1-methyl-N-(1-[(3-methylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
-
compound exhibits good preventive effects against Rhizoctonia solani
3-nitropropanoate
treatment with 3-nitroproprionate dissipates the membrane potential of wild-type or Sdh1 mutant cells under hypoxia but not that of cells grown aerobically
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
4,4,4-trifluoro-1-(2-thienyl)-1,3-butanedione
-
0.006 mM, 50% inhibition
4,4,4-trifluoro-1-(thiophen-2-yl)butane-1,3-dione
-
-
4-Chloromercuriphenyl sulfonate
4-Chloromercuriphenylsulfonate
5,5'-dithiobis(2-nitro-benzoic acid)
-
inactivates, conformation-change type inhibition, the presence of the substrate provides marked protection
5,5'-dithiobis(2-nitrobenzoate)
5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide
i.e., carboxin
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
5-(n-Undecyl)-6-hydroxy-4,7-oxobenzothiazole
-
UHDBT
5-Hydroxy-2-methyl-1,4-naphthoquinone
-
inhibition is only 50% even at 0.1 mM
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
alpha-tocopheryl succinate
-
binds to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
amicarthiazol
i.e. 2-amino-4-methylthiazole -5-carboxanilide, a systemic fungicide. The wild-type enzyme is strongly inhibited by amicarthiazol, while that in resistant mutants is insensitive. A single amino acid substitution H229Y in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, molecular resistance mechanism, overview; i.e. 2-amino-4-methylthiazole-5-carboxanilide, a systemic fungicide. The wild-type enzyme is strongly inhibited by amicarthiazol, while that in resistant mutants is insensitive. A single amino acid substitution H229Y in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, molecular resistance mechanism, overview
antimycin A
-
site of inhibition is located at the oxidation side of cytochrome b
benodanil
-
noncompetitive
Cd2+
-
inhibits possibly due of interfering with energy transport mechanism
Chaotropic reagents
-
e.g. perchlorate, thiocyanate
-
clozapine
-
chronic administration of the antipsychotic agent, inhibit SDH activity only in the striatum
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
fenfuram
-
noncompetitive
ferricyanide
-
at concentrations above 3 mM
flutolanil
-
noncompetitive
furametpyr
-
noncompetitive
haloperidol
-
chronic administration of the antipsychotic agent, inhibits SDH activity in the hippocampus and striatum but not in the cerebellum, cortex, and prefrontal cortex
menaquinone-1
-
competitive inhibitor of the succinate oxidation reaction of succinate dehydrogenase
mepronil
-
noncompetitive
N-[2-(2,4-dichlorophenoxy)phenyl]-3-(difluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
-
compound additionally displays good protection effect against Rhizoctonia solani
N-[2-(2-chloro-4-trifluoromethylphenoxy)phenyl]-3-(2-fluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
-
noncompetitive with respect to 2,6-dichlorophenol indophenol. Compound additionally displays good protection effect against Rhizoctonia solani
nonyl-4-hydroxyquinoline-N-oxide
olanzapine
-
chronic administration of the antipsychotic agent, inhibits SDH activity only in the cerebellum, but not in the hippocampus, striatum, cortex, and prefrontal cortex
oxycarboxin
-
noncompetitive
p-benzoquinone
-
inhibition of succinate dehydrogenase activity using phenazone methosulfate or 2,6-dichlorophenolindophenol as electron acceptor; inhibitory to the succinate dehydrogenase activity assay using phenazine methosulfate and 2,6-dichloroindophenol
p-chloromercuribenzoate
-
-
phenylacetate
unlike N-acetylimidazole and acetylsalicylic acid, phenylacetate is not a donor of acetyl groups. It can be assumed that its effect on SDH may be due to both the activation of acetylation and direct interaction with the enzyme
rotenone
-
inhibits fumarate reductase, not succinate dehydrogenase
sec-butyl-4,6-dinitrophenol
sodium fumarate
-
EC50 fumarate reductase 0.6 mM and EC50 succinate dehydrogenase 4.8 mM
sodium malonate
-
EC50 fumarate reductase 19 mM and EC50 succinate dehydrogenase 0.68 mM
tetrachlorobenzoquinone
strong inhibition of succinate-phenazine methosulfate-(1,4-dichloroindophenol) oxidoreductase
thiabendazole
-
EC50 fumarate reductase 0.46 mM and EC50 succinate dehydrogenase 1 mM
thifluzamide
-
noncompetitive
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]
-
inhibits the enzyme of skeletal muscle and liver
trans-[RuCl2(3,5-pyridinedicarboxylic acid)4]
-
inhibits the enzyme of heart, skeletal muscle, liver, and kidney
trans-[RuCl2(3-pyridinecarboxylic acid)4]
-
inhibits the enzyme of hippocampus, cerebral cortex, heart and liver
trans-[RuCl2(4-pyridinecarboxylic acid)4]
-
inhibits the enzyme of heart and hippocampus
ubiquinol-2
-
competitive inhibitor of the fumarate reduction reaction of fumarate reductase
vitamin E analogues
-
epitomised by alpha-tocopheryl succinate affect the electron flow from complex II
-
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
-
-
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
-
-
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
-
-
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
potent inhibitor that affects both reduction and oxidation of quinone, the inhibitor binds close to heme bD
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
potent inhibitor of fumarate reductase, not inhibitory for succinate dehydrogenase
2-alkyl-4,6-dinitrophenols
-
derivatives of 2-alkyl-4,6-dinitrophenols, competitive inhibitors of both succinate dehydrogenase and fumarate reductase
2-alkyl-4,6-dinitrophenols
-
complete inhibition of the wild-type enzyme and of the mutants H106Y and H113Q
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
-
-
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
-
-
2-heptyl-4-hydroxyquinoline N-oxide
-
more than 0.1 mM, 50% inhibition
2-heptyl-4-hydroxyquinoline N-oxide
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
-
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
site of inhibition is located at the oxidation side of cytochrome b
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
-
2-Thenoyltrifluoroacetone
-
15% inhibition of succinate dehydrogenase activity of larval and adult complex II at 0.1 mM
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
97% inhibition at 0.1 mM
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
slows down the inactivation of the enzyme in the substrate assay mixture
2-Thenoyltrifluoroacetone
-
50% inhibition at 3 mM
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
inhibits both wild-type and carboxin-resistant enzymes, competitive inhibition with respect to quinone
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
-
3'-bromo-carboxin
-
not inhibitory
3'-bromo-carboxin
-
not inhibitory
3'-bromo-carboxin
-
inhibits
3'-fluoro-carboxin
-
not inhibitory
3'-fluoro-carboxin
-
not inhibitory
3'-fluoro-carboxin
-
inhibits
3'-n-butyl-carboxin
-
not inhibitory
3'-n-butyl-carboxin
-
not inhibitory
3'-n-butyl-carboxin
-
inhibits
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
-
-
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
-
-
3-nitropropionic acid
-
irreversible inactivation, 0.00001 mM, 50% inhibition
3-nitropropionic acid
-
this study compares the effects of 3-nitropropionic acid in young and old mice. Treatment with 3-nitropropionic acid induces OD in young mice. Old mice present an increase in the basal level of orofacial movement that is not potentiated by any dose of 3-nitropropionic acid. Histochemical analyses show that old mice present an increase in the SDH activity. 3-Nitropropionic acid induces a decrease in SDH activity at both ages
3-nitropropionic acid
-
-
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
-
-
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
-
-
4-Chloromercuriphenyl sulfonate
-
-
4-Chloromercuriphenyl sulfonate
-
inhibitor of the succinate-ubiquinone reductase reaction
4-Chloromercuriphenyl sulfonate
-
-
4-Chloromercuriphenyl sulfonate
-
inhibits the succinate oxidation by cell-derived particles
4-Chloromercuriphenylsulfonate
-
0.003 mM/g protein 50% inhibition
4-Chloromercuriphenylsulfonate
-
inhibits the oxidation of reduced menaquinone by fumarate. Fumarate reductase, measured with reduced benzylviologen as the donor, is not affected
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
inhibition is reversed by addition of dithiothreitol or dithionite
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
-
-
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
atpenin A4
-
0.00001 mM, 50% inhibition
atpenin A4
-
0.000024 mM, 50% inhibition
atpenin A5
-
0.000004 mM, 50% inhibition
atpenin A5
-
0.0000042 mM, 50% inhibition
atpenin A5
-
0.000004 mM, 50% inhibition
boscalid
-
-
boscalid
-
noncompetitive
carboxin
-
-
carboxin
-
15% inhibition of succinate dehydrogenase activity of larval and adult complex II at 0.001 mM
carboxin
-
not inhibitory
carboxin
-
Q2-mediated Wurster's blue reduction: 90% inhibition at 0.02 mM, Q0-mediated Wurster's blue reduction: 75% inhibition at 0.02 mM, Q1-mediated Wurster's blue reduction: 88% inhibition at 0.02 mM, Q6-mediated Wurster's blue reduction: 50% inhibition at 0.02 mM
carboxin
-
15% inhibition of the succinate-ubiquinone reductase and of the quinol-fumarate reductase reaction, competitive inhibition with quinone or quinol
carboxin
-
0.001 mM, 50% inhibition
carboxin
-
not inhibitory
carboxin
-
inhibits the succinate dehydrogenase in the forward and reverse reaction
carboxin
-
more than 90% inhibition in isolated membranes at high concentrations, the mutant enzyme is less sensitive than wild-type enzyme
carboxin
-
interferes with electron transfer from the 3Fe-4S center to quinone, carboxin may bind to a quinone-binding site the Qp site, close to the 3Fe-4S center, amino acids involved in binding carboxin: a histidine residue in the B subunit and an aspartate residue in the D subunit
carboxin
-
noncompetitive
CN-
-
-
CN-
-
not inhibitory: when mixed with succinate or alone
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
fumarate
-
-
harzianopyridone
-
0.00002 mM, 50% inhibition
harzianopyridone
-
0.0002 mM, 50% inhibition
Maleate
-
-
malonate
-
competitive
malonate
-
inhibits both succinate dehydrogenase and fumarate reductase
malonate
-
0.18 mM, 50% inhibition
malonate
a specific inhibitor of SDH
N-ethylmaleimide
-
-
nonyl-4-hydroxyquinoline-N-oxide
-
-
nonyl-4-hydroxyquinoline-N-oxide
-
the semiquinone analog and inhibitor of quinone reactions in complex II shows no influence on the redox behavior of the heme b moieties
oxaloacetate
-
an inhibitor of the succinate binding site
oxaloacetate
-
competitive inhibitor
oxaloacetate
-
at 0.0006 mM: 20% inhibition of the succinate-ubiquinone reductase reaction and no inhibition of the fumarate reductase reaction, at 0.006 mM: 80% inhibition of fumarate reductase reaction
oxaloacetate
-
reactivation by reduction of enzyme with succinate; reactivation with anions
oxaloacetate
-
reactivation by reduction of enzyme with succinate
oxaloacetate
the interaction between SDH and oxaloacetate renders the enzyme inactive, while the interaction between the activator and enzyme prevent such interaction with oxaloacetate
papyriferic acid
-
papyriferic acid is a triterpene that is secreted by glands on twigs of the juvenile ontogenetic phase of resin producing tree birches. Papyriferic acid is a potent inhibitor of SDH. Kinetic analysis indicate that, unlike malonate, papyriferic acid acts by an uncompetitive mechanism, by binding to the enzyme-substrate complex. The hydrolysis product of papyriferic acid, betulafolienetriol oxide, is inactive on SDH. Papyriferic acid acts as an intact molecule and interacts at a site other than the succinate binding site, possibly binding to the ubiquinone sites on complex II
papyriferic acid
-
papyriferic acid is a triterpene that is secreted by glands on twigs of the juvenile ontogenetic phase of resin producing tree birches. Papyriferic acid is a potent inhibitor of SDH. Kinetic analysis indicate that, unlike malonate, papyriferic acid acts by an uncompetitive mechanism, by binding to the enzyme-substrate complex. The hydrolysis product of papyriferic acid, betulafolienetriol oxide, is inactive on SDH. Papyriferic acid acts as an intact molecule and interacts at a site other than the succinate binding site, possibly binding to the ubiquinone sites on complex II
papyriferic acid
-
papyriferic acid is a triterpene that is secreted by glands on twigs of the juvenile ontogenetic phase of resin producing tree birches. Papyriferic acid is a potent inhibitor of SDH. Kinetic analysis indicate that, unlike malonate, papyriferic acid acts by an uncompetitive mechanism, by binding to the enzyme-substrate complex. The hydrolysis product of papyriferic acid, betulafolienetriol oxide, is inactive on SDH. Papyriferic acid acts as an intact molecule and interacts at a site other than the succinate binding site, possibly binding to the ubiquinone sites on complex II
Pentachlorophenol
-
competitive inhibitor of both succinate dehydrogenase and fumarate reductase
penthiopyrad
-
noncompetitive
penthiopyrad
-
noncompetitie
sec-butyl-4,6-dinitrophenol
-
non-competitive inhibition
sec-butyl-4,6-dinitrophenol
-
-
siccanin
-
-
siccanin
-
residual activity: 7%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
-
residual activity: 13%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
-
residual activity: above 1%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
-
residual activity: 19%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
thenoyltrifluoroacetate
-
inhibits a later step of the electron flow as it binds to the ubiquinone docking sites and abrogates the transfer of electrons to this molecule. It causes a time- and dose-dependent increase of apoptosis. 20% inhibition at 0.5 mM
thenoyltrifluoroacetate
TTFA, a specific inhibitor of SDH
thiol reagents
-
-
additional information
-
transition from darkness to light causes a short transient increase in the SDH activity followed by a decrease to a half of the original activity
-
additional information
-
not inhibitory: thenoyltrifluoroacetone, 2-n-heptyl-4-hydroxyquinoline N-oxide
-
additional information
-
not inhibitory: heptyl 4-hydroxyquinoline N-oxide
-
additional information
-
residual activity: 97%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
-
additional information
-
residual activity: above 77%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
-
additional information
-
different pro-apoptotic agents responsible for complex II inhibition lead to mitochondrial matrix acidification
-
additional information
direct effectors are either deactivators such as oxaloacetate or activators such as substrates, anions, reduced quinone, ATP, and reduction
-
additional information
-
15-20% inhibition of complex II activity in striatum and hippocampus by methylmalonic acid at low concentrations of sucinate in the medium, but not in the peripheral tissue. the inhibitory property only occurs after exposing brain homogenates for at least 10 min with the acid, suggesting that this inhibition is mediated by indirect mechanisms
-
additional information
-
zidovudine, i.e. 3'-azido-3'-deoxythymidine or AZT, represses the enzyme content in mitochondria of cultured rat muscle cells by 13% via reducing the mitochondrial DNA content by 66% at 0.1 mg/ml, histochemic analysis, overview
-
additional information
inhibitory effects of acetylating and deacetylating compounds on the activity of succinate dehydrogenase, as well as effects on the membrane potential and calcium retention capacity of the isolated liver mitochondria, and determination of the possible sites of the enzyme inhibition by the acetylating compounds, overview. Acetylsalicylic acid is the most effective inhibitor of SDH. The inhibition of the enzyme is due to the acetylation of the site binding alpha-ketoglutarate, and it is partially eliminated or prevented by pre-incubation of the mitochondria with nicotinamide adenine dinucleotide, a cofactor for deacetylation, and with polyamine spermidine, an acceptor of acetyl groups. Malonate and thenoyltrifluoroacetate (TTFA), which are specific inhibitors of SDH, as well as the intermediate carrier of electrons phenazine methosulfate (PMS), are used to identify the possible sites of action of these compounds. The influence of NAD, as a cofactor in deacetylation, and polyamine spermidine, as a possible activator of deacetylation, on the modulation of the activity of SDH by acetylating compounds is investigated. PMS prevents the inhibition of SDH caused by TTFA and has no effect on the inhibition induced by malonate. PMS almost completely prevents the inhibition induced by the tested compounds, as does NAD
-
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0.003
2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
value below
0.0034 - 0.018
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
0.12
2,3-dimethyl-1,4-naphthohydroquinone
-
-
0.003 - 0.007
2,6-dichlorophenol indophenol
0.06 - 0.18
caldariellaquinone
0.011
decylubiquinone
-
pH 7.6, 30°C
1.14
ferrocyanide
pH 6.5, 55°C
0.0009 - 0.0054
menaquinol
0.0018 - 0.004
menaquinone
0.0654 - 0.089
oxidized 2,6-dichlorophenolindophenol
0.0991
oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
pH 6.5, 55°C
-
0.295
oxidized phenazine methosulfate
pH 6.5, 55°C
-
0.11 - 0.48
phenazine methosulfate
0.11 - 0.19
reduced plumbagin
0.0016 - 0.02
ubiquinone-1
0.00017 - 0.0114
ubiquinone-2
additional information
fumarate
0.0034
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22°C
0.0037
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22°C
0.0048
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
wild-type
0.007
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
H106Y mutant
0.0073
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
H106L/D117V mutant
0.01
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
F103V mutant
0.011
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
L122stop mutant
0.015
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
H113Q mutant
0.018
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
W116R mutant
0.003
2,6-dichlorophenol indophenol
-
22°C, wild-type strain YPH499
0.007
2,6-dichlorophenol indophenol
-
22°C, Sdh3p/Sdh4p double mutant strain H106A/C78A
0.06
caldariellaquinone
-
pH 6.8, 50°C
0.18
caldariellaquinone
pH 6.5, 55°C
0.3
ferricyanide
-
-
0.005
fumarate
succinate oxidation, pH 7.8, 30°C
0.0054
fumarate
succinate oxidation, pH 7.8, 30°C
0.02
fumarate
wild-type, pH 7.0, 30°C
0.025
fumarate
-
fumarate reduction, Km of fumarate does not depend on concentration of quinol
0.03
fumarate
mutant E49A, pH 7.0, 30°C
0.06
fumarate
pH 6.5, 70°C, detergent treated membranes from aerobic growth
0.06
fumarate
pH 6.5, 70°C, determined for activity in membranes from aerobic growth
0.08
fumarate
pH 6.5, 70°C, detergent treated membranes from anaerobic growth
0.1
fumarate
-
65°C, pH 6.5
0.143
fumarate
-
complex II from adult nematode
0.15
fumarate
-
succinate oxidation
0.35
fumarate
-
donor menadiol
0.455
fumarate
-
complex II from larvae
0.0009
menaquinol
mutant R81A, pH 7.0, 30°C
0.0013
menaquinol
mutant R81E, pH 7.0, 30°C
0.0027
menaquinol
mutant R81K, pH 7.0, 30°C
0.003
menaquinol
mutant R28L, pH 7.0, 30°C
0.0031
menaquinol
mutant R28N, pH 7.0, 30°C
0.0039
menaquinol
mutant R28L/E29L, pH 7.0, 30°C
0.004
menaquinol
mutant R28E/E29I, pH 7.0, 30°C
0.0054
menaquinol
wild-type, pH 7.0, 30°C
0.0018
menaquinone
-
mutant E29L, pH 7.0, 30°C
0.004
menaquinone
-
wild-type, pH 7.0, 30°C
0.0654
oxidized 2,6-dichlorophenolindophenol
pH 6.5, 55°C
0.089
oxidized 2,6-dichlorophenolindophenol
-
pH 6.8, 50°C
0.11
phenazine methosulfate
-
-
0.33
phenazine methosulfate
-
pH 7.6, 30°C
0.48
phenazine methosulfate
-
-
0.48
phenazine methosulfate
-
-
0.11
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101L
0.11
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L
0.124
reduced plumbagin
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L
0.128
reduced plumbagin
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E
0.13
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHB mutant G227L
0.14
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101D
0.16
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95L
0.17
reduced plumbagin
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.19
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95E
0.0015
succinate
fumarate reduction, pH 7.8, 30°C
0.002
succinate
fumarate reduction, pH 7.8, 30°C
0.0025
succinate
-
30°C, pH 7.8
0.03
succinate
-
fumarate reduction
0.04
succinate
-
30°C, pH 7.8, H84L mutant
0.0658
succinate
pH 7.4, 37°C, recombinant Sdh2
0.11
succinate
mutant E49A, pH 7.0, 30°C
0.13
succinate
-
succinate oxidation, determined at 0.01 mM ubiquinone-2
0.138
succinate
-
succinate with papyriferic acid 0.04 mM, pH 7.4, 25°C
0.153
succinate
-
complex II from larvae
0.165
succinate
-
succinate with papyriferic acid 0.04 mM, pH 7.4, 25°C
0.165
succinate
-
65°C, pH 6.5
0.167
succinate
-
succinate with papyriferic acid 0.08 mM, pH 7.4, 25°C
0.21
succinate
-
pH 7.6, 30°C
0.22
succinate
mutant E49A, pH 7.0, 30°C
0.25
succinate
-
30°C, pH 7.0
0.27
succinate
-
for both membrane fragments and mitochondrial enzyme
0.28
succinate
-
pH 6.8, 50°C
0.3
succinate
pH 6.5, 70°C, detergent treated membranes from anaerobic growth
0.303
succinate
-
succinate alone, pH 7.4, 25°C
0.339
succinate
-
succinate alone, pH 7.4, 25°C
0.414
succinate
-
succinate alone, pH 7.4, 25°C
0.5
succinate
pH 6.5, 70°C, detergent treated membranes from aerobic growth
0.5
succinate
pH 6.5, 70°C, determined for activity in membranes from aerobic growth
0.55
succinate
wild-type, pH 7.0, 30°C
0.608
succinate
-
complex II from adult nematode
0.64
succinate
-
pH 7.6, 30°C
0.7
succinate
-
membrane bound enzyme
1.42
succinate
pH 6.5, 55°C
2.3
succinate
-
soluble enzyme
0.0005
ubiquinone
mutant R81E, pH 8.0, 30°C
0.0006
ubiquinone
mutant R81A, pH 8.0, 30°C
0.0013
ubiquinone
mutant R81K, pH 8.0, 30°C
0.0015
ubiquinone
mutant R28L, pH 8.0, 30°C
0.0015
ubiquinone
mutant R28N, pH 8.0, 30°C
0.002
ubiquinone
mutant R28L/E29L, pH 8.0, 30°C
0.0023
ubiquinone
wild-type, pH 8.0, 30°C
0.0025
ubiquinone
-
wild-type SQR
0.0038
ubiquinone
mutant R28E/E29I, pH 8.0, 30°C
0.01
ubiquinone
-
mutant H71Y
0.01
ubiquinone
-
mutant E29F, pH 7.9, 30°C
0.012
ubiquinone
-
mutant H71Y
0.013
ubiquinone
-
mutant H71Y/A72C
0.014
ubiquinone
-
mutant enzyme
0.017
ubiquinone
-
wild-type enzyme
0.027
ubiquinone
-
mutant E29L, pH 7.9, 30°C
0.06
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L
0.07
ubiquinone
-
wild-type, pH 7.9, 30°C
0.07
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95L
0.09
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHB mutant G227L
0.09
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101L
0.1
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101D
0.13
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95E
0.15
ubiquinone
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.16
ubiquinone
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L
0.2
ubiquinone
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E
0.0016
ubiquinone-1
-
-
0.003
ubiquinone-1
-
larval and adult complex II
0.02
ubiquinone-1
-
pH 6.8, 50°C
0.00017
ubiquinone-2
-
differences in Km value (9fold) and Vmax/Km ratio (19fold) between Q1 and Q2 indicate that the 6-polyprenyl tail of the ubiquinone ring contributes to the binding affinity and that Q2 is better substrate than Q1
0.0089
ubiquinone-2
-
S33C mutant
0.009
ubiquinone-2
-
R19A and F20L mutants
0.01
ubiquinone-2
-
S33T mutant
0.0102
ubiquinone-2
-
T17A mutant
0.0106
ubiquinone-2
-
H30A mutant
0.0108
ubiquinone-2
-
wild-type and T23A mutant
0.0114
ubiquinone-2
-
S33A mutant
additional information
fumarate
-
with menaquinone EC 1.3.5.4, succinate oxidation: 0.003 mM, pH 7.8, 30°C
additional information
fumarate
with menaquinone EC 1.3.5.4, succinate oxidation: 0.003 mM, pH 7.8, 30°C
additional information
additional information
-
succinate-quinone and quinol-fumarate reductase reaction of succinate dehydrogenase and fumarate reductase
-
additional information
additional information
-
no effect of phosphate on fumarate reductase, but increase of Km of succinate dehydrogenase
-
additional information
additional information
-
midpoint potentials of [3Fe-4S] cluster and heme b, kinetics and kinetic isotope effects of recombinant wild-type and mutant enzymes at different pH in both reaction directions, overview
-
additional information
additional information
-
interprotomer temperature-dependent positive cooperativity in the trimeric complex. Only the trimer, not the monomer, exhibits positive cooperativity at high temperatures
-
additional information
additional information
-
steady-state kinetic measurements show that the enzyme displays standard Michaelis-Menten kinetics at a low temperature of 30°C but exhibits deviation from it at a higher temperature of 70°C, the enzyme shows positive cooperativity at higher temperatures
-
additional information
succinate
-
fumarate reduction. 0.0013 mM, with ubiquinone, reaction of succinate-ubiquinone oxidase EC 1.3.5.1
additional information
succinate
fumarate reduction. 0.0013 mM, with ubiquinone, reaction of succinate-ubiquinone oxidase EC 1.3.5.1
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3.67
1,4-Naphthoquinone
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30°C
35 - 182
2,3-dimethoxy-5-methyl-1,4-benzoquinone
3.6 - 60
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
9.4 - 29.6
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
2.167
duroquinone
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30°C
1.67
menadione
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30°C
1.83
oxidized 2,6-dichlorophenolindophenol
-
pH 7.6, 30°C
82
oxidized phenazine ethosulfate
-
30°C, pH 7.8
-
8.33 - 77
phenazine methosulfate
7.7 - 23
reduced plumbagin
additional information
fumarate
35
2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
isolated complex
182
2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
membrane preparation
3.6
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22°C
60
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22°C
9.4
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L
12.6
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101L
15.9
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25°C, recombinant subunit SDHB mutant G227L
17.4
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95L
18
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101D
19.9
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E
20.8
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L
20.9
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25°C, recombinant wild-type enzyme
29.6
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95E
20.1
ferricyanide
mutant R28L/R81A, pH 8.0, 30°C
24.6
ferricyanide
mutant R28N, pH 8.0, 30°C
26.4
ferricyanide
mutant R28E/E29I, pH 8.0, 30°C
27.1
ferricyanide
mutant R28L, pH 8.0, 30°C
27.3
ferricyanide
mutant R81E, pH 8.0, 30°C
28.1
ferricyanide
mutant R81A, pH 8.0, 30°C
28.7
ferricyanide
wild-type, pH 8.0, 30°C
28.9
ferricyanide
mutant R28L/E29L, pH 8.0, 30°C
30.4
ferricyanide
mutant R81K, pH 8.0, 30°C
0.3
fumarate
-
mutant K228R, cosubstrate menaquinone, pH 7.0, 30°C
1
fumarate
mutant E49A, pH 7.0, 30°C
1.7
fumarate
succinate oxidation, pH 7.8, 30°C
2.3
fumarate
-
mutant E49F, cosubstrate menaquinone, pH 7.0, 30°C
5
fumarate
-
mutant E49L, cosubstrate menaquinone, pH 7.0, 30°C
20
fumarate
-
based on the content of the MW 79000 peptide, reduction of fumarate with dimethylnaphthohydroquinone
32
fumarate
mutant E49A, pH 7.0, 30°C
79.6
fumarate
-
65°C, pH 6.5
133
fumarate
-
with 2,3-dimethyl-1,4-naphthohydroquinone, based on FAD content of enzyme
177
fumarate
succinate oxidation, pH 7.8, 30°C
230
fumarate
-
wild-type, cosubstrate menaquinone, pH 7.0, 30°C
250
fumarate
wild-type, pH 7.0, 30°C
2.8
menaquinol
mutant R28E/E29I, pH 8.0, 30°C
3
menaquinol
mutant R28E/E29I, pH 7.0, 30°C
6.1
menaquinol
mutant R81A, pH 8.0, 30°C
10.6
menaquinol
mutant R81A, pH 7.0, 30°C
11.1
menaquinol
mutant R28L/E29L, pH 8.0, 30°C
12.2
menaquinol
mutant R28L/E29L, pH 7.0, 30°C
12.8
menaquinol
mutant R81E, pH 8.0, 30°C
14
menaquinol
mutant R81E, pH 7.0, 30°C
65.4
menaquinol
mutant R28N, pH 8.0, 30°C
67.8
menaquinol
mutant R28L, pH 8.0, 30°C
68.6
menaquinol
mutant R28N, pH 7.0, 30°C
71.1
menaquinol
mutant R28L, pH 7.0, 30°C
123.7
menaquinol
mutant R81K, pH 7.0, 30°C
138.9
menaquinol
mutant R81K, pH 8.0, 30°C
211
menaquinol
wild-type, pH 8.0, 30°C
222.2
menaquinol
wild-type, pH 7.0, 30°C
0.2
naphthoquinol
-
mutant enzyme
2
naphthoquinol
-
wild-type enzyme
8.33
phenazine methosulfate
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30°C
77
phenazine methosulfate
-
pH 7.6, 30°C
7.7
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101L
8.6
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95L
9.1
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHB mutant G227L
9.3
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L
10.4
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101D
12.7
reduced plumbagin
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95E
15.9
reduced plumbagin
-
pH 8.0, 25°C, recombinant wild-type enzyme
21.5
reduced plumbagin
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L
23
reduced plumbagin
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E
0.1
succinate
-
mutant K228R, cosubstrate ubiquinone, pH 7.9, 30°C
0.3
succinate
-
mutant E49L, cosubstrate menaquinone, pH 7.9, 30°C
0.3
succinate
-
mutant K228L, cosubstrate ubiquinone, pH 7.9, 30°C
0.4
succinate
-
mutant E49F, cosubstrate menaquinone, pH 7.9, 30°C
2.4
succinate
mutant E49A, pH 7.0, 30°C
3.16
succinate
pH 7.4, 37°C, recombinant Sdh2
4
succinate
mutant E49A, pH 7.0, 30°C
10
succinate
-
mutant enzyme
13
succinate
-
with 2,3-dimethyl-1,4-naphthoquinone, based on FAD content of enzyme
14
succinate
fumarate reduction, pH 7.8, 30°C
15
succinate
-
wild-type, cosubstrate menaquinone, pH 7.9, 30°C
20.4
succinate
-
mutant E49F, cosubstrate ubiquinone, pH 7.9, 30°C
23
succinate
-
mutant E49L, cosubstrate ubiquinone, pH 7.9, 30°C
24
succinate
-
wild-type, cosubstrate ubiquinone, pH 7.9, 30°C
30
succinate
wild-type, pH 7.0, 30°C
78
succinate
-
30°C, pH 7.8
80
succinate
-
reaction with phenazine methosulfate and 2,6-dichlorophenolindophenol
83.3 - 150
succinate
-
based on FAD content, dependency on assay temperature
85
succinate
fumarate reduction, pH 7.8, 30°C
260
succinate
-
wild-type enzyme
1.7
ubiquinone
mutant R28E/E29I, pH 8.0, 30°C
10.7
ubiquinone
mutant R81E, pH 8.0, 30°C
11.6
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHB mutant G227L
13.9
ubiquinone
mutant R28L/E29L, pH 8.0, 30°C
15.6
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101L
16.2
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95L
17.4
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L
17.4
ubiquinone
mutant R81A, pH 8.0, 30°C
18.6
ubiquinone
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E
19
ubiquinone
mutant R28N, pH 8.0, 30°C
19.3
ubiquinone
mutant R28L, pH 8.0, 30°C
20.9
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant E101D
22.3
ubiquinone
-
pH 8.0, 25°C, recombinant subunit SDHC mutant D95E
24.8
ubiquinone
-
pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L
24.9
ubiquinone
wild-type, pH 8.0, 30°C
32.2
ubiquinone
mutant R81K, pH 8.0, 30°C
37.9
ubiquinone
-
pH 8.0, 25°C, recombinant wild-type enzyme
additional information
fumarate
-
with menaquinone EC 1.3.5.4: , succinate oxidation: 3.4 s-1, pH 7.8, 30°C
additional information
fumarate
with menaquinone EC 1.3.5.4: , succinate oxidation: 3.4 s-1, pH 7.8, 30°C
additional information
additional information
-
-
-
additional information
additional information
-
succinate-quinone and quinol-fumarate reductase reaction of succinate dehydrogenase and fumarate reductase
-
additional information
succinate
-
fumarate reduction. 28 s-1, with ubiquinone, reaction of succinate-ubiquinone oxidase EC 1.3.5.1
additional information
succinate
fumarate reduction. 28 s-1, with ubiquinone, reaction of succinate-ubiquinone oxidase EC 1.3.5.1
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0.00011 - 0.00233
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
0.00033 - 0.03
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
0.00063 - 0.03
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
0.00001 - 0.000051
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
0.00013 - 0.000234
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
0.0001 - 0.00258
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
0.00002 - 0.000122
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
0.000003 - 0.000004
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
0.00001 - 0.000299
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
0.03
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
0.0128 - 0.0207
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
0.03
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
0.00045 - 0.00298
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
0.03
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
0.00049 - 0.00408
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
0.0006 - 0.00061
2-bromo-3-ethyl-1,4-naphthoquinone
0.000061 - 0.00109
2-bromo-3-methyl-1,4-naphthoquinone
0.00127 - 0.00194
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
0.00001 - 0.000024
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
0.00004
3-(difluoromethyl)-1-methyl-N-(1-[(3,5-dimethylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.03
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
0.0138 - 0.0139
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
0.03
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
0.03
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
0.0008 - 0.00275
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
0.03
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
0.00656 - 0.03
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
0.0034 - 0.0267
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
0.000004 - 0.0046
atpenin A5
0.0128
benodanil
Sus scrofa
-
pH 7.4,23°C
0.000245 - 0.0083
boscalid
0.00013 - 0.00178
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
0.1233
fenfuram
Sus scrofa
-
pH 7.4,23°C
0.0289
flutolanil
Sus scrofa
-
pH 7.4,23°C
0.0273
furametpyr
Sus scrofa
-
pH 7.4,23°C
0.0304
mepronil
Sus scrofa
-
pH 7.4,23°C
0.0004
N-[2-(2,4-dichlorophenoxy)phenyl]-3-(difluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.000062
N-[2-(2-chloro-4-trifluoromethylphenoxy)phenyl]-3-(2-fluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.0856
oxycarboxin
Sus scrofa
-
pH 7.4,23°C
0.00053 - 0.0013
penthiopyrad
0.00017
thifluzamide
Sus scrofa
-
pH 7.4,23°C
0.00011
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
Bos taurus
-
-
0.00233
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
Parastagonospora nodorum
-
-
0.00033
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
Bos taurus
-
-
0.03
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
Parastagonospora nodorum
-
value above
0.00063
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
Bos taurus
-
-
0.03
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
Parastagonospora nodorum
-
value above
0.00001
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
Bos taurus
-
-
0.000051
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
Parastagonospora nodorum
-
-
0.00013
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
Bos taurus
-
-
0.000234
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
Parastagonospora nodorum
-
-
0.0001
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
Bos taurus
-
-
0.00258
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
Parastagonospora nodorum
-
-
0.00002
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
Bos taurus
-
-
0.000122
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
Parastagonospora nodorum
-
-
0.000003
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
Bos taurus
-
-
0.000004
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
Parastagonospora nodorum
-
-
0.00001
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
Bos taurus
-
-
0.000299
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
Parastagonospora nodorum
-
-
0.03
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
Bos taurus
-
value above
0.03
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
Parastagonospora nodorum
-
value above
0.0128
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
Bos taurus
-
-
0.0207
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
Parastagonospora nodorum
-
-
0.03
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
Bos taurus
-
value above
0.03
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
Parastagonospora nodorum
-
value above
0.00045
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
Bos taurus
-
-
0.00298
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
Parastagonospora nodorum
-
-
0.03
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
Bos taurus
-
value above
0.03
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
Parastagonospora nodorum
-
value above
0.00049
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
Bos taurus
-
-
0.00408
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
Parastagonospora nodorum
-
-
0.0006
2-bromo-3-ethyl-1,4-naphthoquinone
Wolinella succinogenes
inhibition of quinone reduction by succinate, pH 7.4, 37°C
0.00061
2-bromo-3-ethyl-1,4-naphthoquinone
Wolinella succinogenes
inhibition of quinol oxidation by fumarate, pH 7.4, 37°C
0.000061
2-bromo-3-methyl-1,4-naphthoquinone
Wolinella succinogenes
inhibition of quinol oxidation by fumarate, pH 7.4, 37°C
0.00109
2-bromo-3-methyl-1,4-naphthoquinone
Wolinella succinogenes
inhibition of quinone reduction by succinate, pH 7.4, 37°C
0.00127
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
Bos taurus
-
-
0.00194
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
Parastagonospora nodorum
-
-
0.00001
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
Bos taurus
-
-
0.000024
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
Parastagonospora nodorum
-
-
0.03
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
Bos taurus
-
value above
0.03
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
Parastagonospora nodorum
-
value above
0.0138
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
Bos taurus
-
-
0.0139
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
Parastagonospora nodorum
-
-
0.03
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
Bos taurus
-
value above
0.03
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
Parastagonospora nodorum
-
value above
0.03
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
Bos taurus
-
value above
0.03
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
Parastagonospora nodorum
-
value above
0.0008
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
Bos taurus
-
-
0.00275
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
Parastagonospora nodorum
-
-
0.03
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
Bos taurus
-
value above
0.03
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
Parastagonospora nodorum
-
value above
0.00656
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
Bos taurus
-
-
0.03
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
Parastagonospora nodorum
-
value above
0.0034
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
Bos taurus
-
-
0.0267
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
Parastagonospora nodorum
-
-
0.000004
atpenin A5
Bos taurus
-
-
0.000011
atpenin A5
Parastagonospora nodorum
-
-
0.0046
atpenin A5
Plasmodium yoelii yoelii
-
-
0.000245
boscalid
Parastagonospora nodorum
-
-
0.00179
boscalid
Bos taurus
-
-
0.0083
boscalid
Sus scrofa
-
pH 7.4,23°C
0.0036
carboxin
Plasmodium yoelii yoelii
-
-
0.0043
carboxin
Sus scrofa
-
pH 7.4,23°C
0.00013
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
Bos taurus
-
-
0.00178
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
Parastagonospora nodorum
-
-
0.00053
penthiopyrad
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.00124
penthiopyrad
Sus scrofa
-
pH 7.4,23°C
0.0013
penthiopyrad
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.0009
siccanin
Pseudomonas aeruginosa
-
pH 7.4, 25°C
0.009
siccanin
Rattus norvegicus
-
pH 7.4, 25°C
0.21
siccanin
Escherichia coli
-
-
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evolution
-
the enzyme as respiratory complex II belongs to the succinate:quinone oxidoreductases superfamily that comprises succinate:quinone reductases and quinol:fumarate reductases
evolution
enzyme QFR is a member of the complex II superfamily and is composed of FrdABCD subunits
evolution
Megalodesulfovibrio gigas
one menaquinone molecule is bound near heme bL in the hydrophobic subunit C. This location of the menaquinone-binding site differs from the menaquinol-binding cavity proposed previously for QFR from Wolinella succinogenes. The observed bound menaquinone might serve as an additional redox cofactor to mediate the proton-coupled electron transport across the membrane
evolution
quinol:fumarate reductase (QFR) is a member of the respiratory complex II superfamily
evolution
-
the SDH function is regulated through distinct molecular pathways in different species
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
-
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
evolution
Megalodesulfovibrio gigas DSM 1382
-
one menaquinone molecule is bound near heme bL in the hydrophobic subunit C. This location of the menaquinone-binding site differs from the menaquinol-binding cavity proposed previously for QFR from Wolinella succinogenes. The observed bound menaquinone might serve as an additional redox cofactor to mediate the proton-coupled electron transport across the membrane
-
evolution
-
the enzyme as respiratory complex II belongs to the succinate:quinone oxidoreductases superfamily that comprises succinate:quinone reductases and quinol:fumarate reductases
-
malfunction
-
the frequency of polymorphisms of SDHs, hypoxia-inducible factor type 1 and angiotensin converting enzyme genes is compared between 40 subjects with intolerance to high altitude and a low hypoxic ventilatory response at exercise and 41 subjects without intolerance to high altitude and a high hypoxic ventilatory. No significant association between low or high hypoxic ventilatory response and the allele frequencies for nine single nucleotide polymorphisms in the SDHD and SDHB genes, the ACE insertion/deletion polymorphism and four single nucleotide polymorphisms in the hypoxia-inducible factor type 1 a gene is found. No clear association is found between gene variants involved in oxygen sensing and chemoresponsiveness, although some mutations in the SDHB and SDHD genes deserve further investigations in a larger population
malfunction
-
the presentation of three synchronous extra-adrenal abdominal paragangliomas in an adolescent boy who carries a germline mutation in the SDHB gene are reported. Loss of heterozygosity of this allele is demonstrated by direct sequencing of DNA from two of his tumors, confirming loss of tumor suppressor function in the pathogenesis of these paragangliomas
malfunction
-
the succinate:ubiquinone oxidoreductase activity of the mitochondrial respiratory complex II is specifically impaired by reactive oxygen species without affecting the second enzymatic activity of this complex as a succinate dehydrogenase. The different pro-apoptotic agents responsible for complex II inhibition lead to mitochondrial matrix acidification. Complex II contributes to apoptosis induction only when the SQR activity is inhibited while the SDH activity is still fully functioning,creating an uncoupling phenomenon at the complex II level. The association of an active SDH activity with an inhibited SQR function is not possible, rendering complex II incapable of apoptosis induction and promoting tumourigenesis
malfunction
impaired function of SDH results in deleterious disorders from cancer to neurodegeneration. Defective SDH leads to tumorigenesis, where accumulated succinate promotes HIF-1 stabilization. In humans, another regulatory mechanism through alternative splicing of SDHC transcript is reported in which a shorter isoform of SDHC (DELTA5 lacking exon 5) is produced which lacks heme binding region and therefore has no function. This results in significant downregulation of SDH complex. This variant of SDHC may, therefore, act as a dominant-negative inhibitor of full-length SDHC. DELAT5 may have a role in the pathogenesis of tumorigenesis associated with the malfunction of SDH. A posttranscriptional regulation has been described in late stages of lung cancer in which miR-210 (a microRNA) is overexpressed in normoxia. miR-210 targets SDHD and other transcripts of complex I and II such as NDUAF4 eventually leading to mitochondrial dysfunction and cell death. miR-210-dependent targeting of SDHD transcript activates HIF-1 and in agreement with earlier findings links loss-of-function SDH mutations to HIF-1 stabilization. A mutation in K547 of SDHA (which is typically desuccinylated by SIRT5) renders SDHA unable to interact with SDH5 and thereby made SDH inactive. Furthermore, SIRT5 promotes clear cell renal cell carcinoma (ccRCC) proliferation through inactivation of SDH and switching metabolism to aerobic glycolysis
malfunction
the yeast cells lacking SDH5 gene can grow in fermentative mode (i.e. in glucose), but fail to grow in respiratory mode (e.g. in glycerol) which is an indication of a defective oxidative phosphorylation. This phenotype can be rescued by expression of SDH5. Other phenotypes of sdh5DELTA yeast cells include: substantially decreased levels of all four SDH subunits, impaired oxygen consumption (similar to the respiratory-deficient sdh1DELTA cells), respiration-related phenotypes of H2O2 hypersensitivity and reduced chronological life-span. Another phenotype is acetate hyper-excretion which is shared by four other TCA cycle mutants. A yeast strain lacking SDHAF1 homologue Sdh6 is OXPHOS incompetent. Transformation of this strain with YDR379C-A variants corresponding to the human mutant alleles do not recover OXPHOS growth, indicating that these mutations cause the disease. Yeast lacking SDHAF3 exhibits defective SDH activity and reduced levels of Sdh2
metabolism
-
enzymatic activity, quinone content and complex II subunit composition in mitochondria of lung stage L3 (LL3) Ascaris suum larvae is examined. Lung stage L3 Ascaris suum larvae mitochondria show higher quinolfumarate reductase activity than mitochondria of Ascaris suum at other stages. Ubiquinone content in lung stage L3 larvae mitochondria is more abundant than rhodoquinone. It is shown that lung stage L3 larvae mitochondria contain larval flavoprotein subunit (Fp) and adult flavoprotein subunit at a ratio of 1:0.56, and that most lung stage L3 larvae cytochrome b containing subunits CybS are of the adult form. This clearly indicates that the rearrangement of complex II begins with a change in the isoform of the anchor CybS subunit, followed by a similar change in the Fp subunit
metabolism
Megalodesulfovibrio gigas
QFR catalyzes the coupled reduction of fumarate to succinate with the oxidation of hydroquinone (quinol) to quinone on opposite sides of the inner cytoplasmic membrane. The reverse reaction, namely, the coupled oxidation of succinate to fumarate with the reduction of quinone to quinol, is catalyzed by the well-studied succinate:quinone reductase (SQR, EC 1.3.5.1), often referred to as complex II in the respiratory electron-transport chain of aerobic organisms
metabolism
succinate dehydrogenase (SDH) is one of the most important enzymes involved in the in three cellular processes: glycolysis, the tricarboxylic acid cycle (TCA cycle, Krebs cycle) and oxidative phosphorylation (OXPHOS). SDH, also known as complex II or succinate:ubiquinone oxidoreductase (SQR) is a unique enzyme in four ways: first, it is involved in both the TCA and OXPHOS in mitochondria. Second, all the genes for mitochondrial SDH are nuclear. Third, it is the only membrane-bound component of TCA cycle. Fourth, it is the smallest and the only complex of mitochondrial electron transport chain (ETC) which does not directly extrude protons. But it contributes to the proton gradient by supplying reducing equivalents resulting from succinate metabolism. The reducing equivalents are then transported through the ubiquinone pool thereby enabling proton extrusion by complex III and IV
metabolism
succinate dehydrogenase (SDH) is one of the most important enzymes involved in the three cellular processes: glycolysis, the tricarboxylic acid cycle (TCA cycle, Krebs cycle) and oxidative phosphorylation (OXPHOS). SDH, also known as complex II or succinate:ubiquinone oxidoreductase (SQR) is a unique enzyme in four ways: first, it is involved in both the TCA and OXPHOS in mitochondria. Second, all the genes for mitochondrial SDH are nuclear. Third, it is the only membrane-bound component of TCA cycle. Fourth, it is the smallest and the only complex of mitochondrial electron transport chain (ETC) which does not directly extrude protons. But it contributes to the proton gradient by supplying reducing equivalents resulting from succinate metabolism. The reducing equivalents are then transported through the ubiquinone pool thereby enabling proton extrusion by complex III and IV. Succinate is oxidized to fumarate in the TCA cycle by SDHA-B and the electrons derived are transported to ubiquinone (coenzyme Q) and then to complex III. The electrons along the way reduce FAD of SDHA subunit and move through Fe-S clusters in SDHB subunit and then reduce ubiquinone before transfer to complex III
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
metabolism
succinate:quinone oxidoreductase (SQR) functions in energy metabolism, coupling the tricarboxylic acid cycle and electron transport chain in bacteria and mitochondria. The biogenesis of flavinylated SdhA, the catalytic subunit of SQR, is assisted by a highly conserved assembly factor termed SdhE in bacteria via an unknown mechanism. Bacterial SdhE proteins, and their mitochondrial homologues, seem to be assembly chaperones that constrain the conformation of SdhA to facilitate efficient flavinylation while regulating succinate dehydrogenase activity for productive biogenesis of SQR
metabolism
Megalodesulfovibrio gigas DSM 1382
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QFR catalyzes the coupled reduction of fumarate to succinate with the oxidation of hydroquinone (quinol) to quinone on opposite sides of the inner cytoplasmic membrane. The reverse reaction, namely, the coupled oxidation of succinate to fumarate with the reduction of quinone to quinol, is catalyzed by the well-studied succinate:quinone reductase (SQR, EC 1.3.5.1), often referred to as complex II in the respiratory electron-transport chain of aerobic organisms
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physiological function
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the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional
physiological function
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the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional
physiological function
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the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional
physiological function
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using pharmacological and siRNA methodologies it is shown that increased methylation of histone H3 is a general consequence of SDH loss-of-function in cultured mammalian cells and can be reversed by overexpression of the JMJD3 histone demethylase. ChIP analysis reveals that the core promoter of IGFBP7, which encodes a secreted protein upregulated after loss of SDHB, shows decreased occupancy by H3K27me3 (histone 3 methylated on residue K27) in the absence of SDH
physiological function
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using the submitochondrial particles from the adult worms and L3 larvae of the parasitic nematode Ascaris suum, it is shown that reactive oxygen species are produced from the flavin adenine dinucleotide-binding site as well as the quinone binding site in the mitochondrial complex II
physiological function
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enzyme belongs to a system of electron transport phosphorylation in which formate functions as the donor and fumarate as the terminal acceptor. Menaquinone is an obligatory redox mediator of formate-fumarate reductase electron transport phosphorylation system
physiological function
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fumarate reductase, which is proficient in succinate oxidation, is able to functionally replace succinate-ubiquinone oxidoreductase in aerobic respiration when conditions are used to allow the expression of the frdABCD operon aerobically. Expression of plasmids which utilize the FRD promoter of the frdABCD operon fused to the sdhCDAB genes to drive expression shows that, under anaerobic growth conditions where fumarate is utilized as the terminal electron acceptor, succinate-ubiquinone oxidoreductase would function to support anaerobic growth of Escherichia coli
physiological function
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fumarate reduction by NADH is catalyzed by an electron transport chain consisting of NADH dehydrogenase NADH:menaquinone reductase, menaquinone, and succinate dehydrogenase operating in the reverse direction, i.e. menaquinol:fumarate reductase. In sdh or aro mutant strains, which lack succinate dehydrogenase or menaquinone, respectively, the activity of fumarate reduction by NADH is missing. The membrane fraction of a mutant lacking functional sdh genes catalyzes fumarate reduction by NADH or 2,3-dimethyl-1,4-naphthoquinol with less than 7% of the wild-type activities. In resting cells fumarate reduction requires glycerol or glucose as the electron donor, which presumably supply NADH for fumarate reduction
physiological function
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is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate
physiological function
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the enzyme is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain
physiological function
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the enzyme is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain
physiological function
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the enzyme is involved in anaerobic metabolism
physiological function
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the enzyme is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate
physiological function
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the FrdD subunit has an essential role both in the interaction of the enzyme with reduced menaquinone and thus in anaerobic respiration with fumarate as electron acceptor, and in binding the enzyme to the membrane
physiological function
the QFR complex provides electron transport during anaerobic cell growth conditions. The transcription of the frdABCD operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the succinate-ubiquinone oxidase, EC 1.3.5.1, overview
physiological function
the SQR complex provides electron transport during aerobic cell growth conditions. The transcription of the sdhCDAB operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the menaquinol-fumarate oxidoreductase, EC 1.3.5.4, overview
physiological function
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succinate:quinone reductase serves as the respiratory complex II
physiological function
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succinate:ubiquinone oxidoreductase is part of the mitochondrial respiratory complex II
physiological function
the enzyme is involved in electron transfer via the respiratory chain
physiological function
the enzyme is part of the complex II, which in the anaerobic respiratory chain of the parasitic nematode Ascaris suum, couples the reduction of fumarate to the oxidation of rhodoquinol. Critical role of the low redox potential of rhodoquinol in the fumarate reduction of Ascaris suum complex II
physiological function
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a subunit MfrA mutant strain is less susceptible to H2O2 as the wildtype. The H2O2 concentration in the mutant cultures is significantly higher than that of wild-type. In the presence of H2O2, catalase activity and expression are lower in the mutant strain as compared to the wild-type. Exposure to H2O2 results in a significant decrease in total intracellular iron in the mutant strain, while the addition of iron to the growth medium mitigates H2O2 susceptibility and accumulation in the mutant. The mutant strain is significantly more persistent in RAW macrophages
physiological function
deletion of the sdh1 operon does not yield any growth phenotypes on succinate or other nonfermentable carbon sources
physiological function
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overexpression of SdhC and SdhD suppresses 1-(4-chlorophenyl)-benzo-2,5-quinone-induced inhibition of complex II activity, increase in mitochondrial levels of reactive oxygen species, and toxicity
physiological function
presence of the Sdh2 operon is essential for growth. Isoform Sdh2 is the generator of the membrane potential under hypoxia
physiological function
acetylation can participate in the modulation of the enzymatic activity of SDH, a key enzyme of the tricarboxylic acid cycle, along with the well-known mechanisms of inhibition by oxaloacetic acid, oxidative stress, or mutations in enzyme subunits, in maintaining the energy supply, membrane potential, and other functions of mitochondria
physiological function
in addition to its role in bioenergetics, QFR binds to the FliG subunit of the switch-motor of the bacterial flagellar rotor and promotes clockwise rotation of the flagellum, which is essential for chemotaxis
physiological function
quinol:fumarate reductase (QFR, FrdABCD) catalyzes the interconversion of fumarate and succinate at a covalently attached FAD within the FrdA subunit. The SdhE assembly factor enhances covalent flavinylation of complex II homologues, mechanism, overview. QFR catalyzes the reduction of fumarate (kcat = 250/s) at this flavin-based active site during anaerobic respiration with fumarate as the terminal electron acceptor. In this process, the two electrons for fumarate reduction derived from the oxidation of menaquinol in the membrane and the two protons are likely transferred from solvent via a proton shuttle pathway consisting of the FrdA-E245, FrdA-R248, and FrdA-R287 side chains located on the capping domain. QFR can also catalyze the reverse reaction, succinate oxidation, albeit with slower kinetics (kcatx02= 30/s) and poorer catalytic efficiency
physiological function
succinate dehydrogenase (SDH) is a protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, overview
physiological function
succinate dehydrogenase (SDH) is an inner mitochondrial membrane protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, detailed overview. Oxidation state transitions involve a one- or two-electron redox reaction, each being thermodynamically constrained. When the quinone reductase site is inhibited or the quinone pool is highly reduced, superoxide is generated primarily by the FAD. In addition, H2O2 production is only significant when the enzyme is fully reduced, and fumarate is absent. SDH significantly contributes to total mitochondrial ROS production
physiological function
succinate dehydrogenase (SDH) is an inner mitochondrial membrane protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, detailed overview. Oxidation state transitions involve a one- or two-electron redox reaction, each being thermodynamically constrained. When the quinone reductase site is inhibited or the quinone pool is highly reduced, superoxide is generated primarily by the FAD. In addition, H2O2 production is only significant when the enzyme is fully reduced, and fumarate is absent. SDH significantly contributes to total mitochondrial ROS production
physiological function
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. Enzyme regulation can occur via transcription factors, post-transcriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In bacteria alteration of SDH expression by aerobiosis/anaerobiosis and various carbon sources is also implemented through transcriptional regulation. In this case fnr and arcA gene products both act to repress SDHC expression in response to oxygen. In Escherichia coli a EIICBGlc protein (the ptsG gene product) is identified, that is a component of the major glucose transport machinery known as phosphoenolpyruvate (PEP) phosphotransferase system (PTS), and a crucial mediator of the repression of the sdhCDAB operon in the presence of glucose. It acts via the transcription factor crp, which directly regulates expression of the sdhCDAB operon. The glucose repression of this operon occurs in a cAMP-dependent manner
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In bacteria alteration of SDH expression by aerobiosis/anaerobiosis and various carbon sources is also implemented through transcriptional regulation. In this case fnr and arcA gene products both act to repress SDHC expression in response to oxygen
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In bacteria alteration of SDH expression by aerobiosis/anaerobiosis and various carbon sources is also implemented through transcriptional regulation. In this case fnr and arcA gene products both act to repress SDHC expression in response to oxygen
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In bacteria alteration of SDH expression by aerobiosis/anaerobiosis and various carbon sources is also implemented through transcriptional regulation. In this case fnr and arcA gene products both act to repress SDHC expression in response to oxygen. In Neisseria meningitides low iron condition leads to high expression of NrrF. The latter is an sRNA that targets sdhCDAB transcript and promotes its degradation with the assistance of Hfq chaperone. The concentration of iron is sensed by Fur which represses the genes responsible for iron uptake with the assistance of ferrous iron as a corepressor
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In bacteria alteration of SDH expression by aerobiosis/anaerobiosis and various carbon sources is also implemented through transcriptional regulation. In this case, fnr and arcA gene products both act to repress SDHC expression in response to oxygen
physiological function
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In yeast, glucose represses the transcription of SDH2 (SDHB homologue) by a mechanism in which the upstream promoter sequence of SDHB containing four regulatory elements is shown to interact with the HAP2/3/4 transcription activator complex. Maximum expression of SDH1 (SDHA homologue) and SDH3 (SDHC homologue) require the same transcription activator. Accordingly, the expression of SDH1 and SDH3 is enhanced 5 times more strongly on galactose than on glucose. Likewise, an increase in the abundance of SDH4 (SDHD homologue) mRNA observed in media containing galactose rather than glucose. Therefore it seems that the same transcription activator complex regulates the transcription of all 4 genes encoding subunits of SDH. The 5'-untranslated region (5' UTR) of the SDH2 mRNA contains a major determinant which controls its differential turnover in media containing glycerol versus glucose. Furthermore, the 5' exonuclease encoded by the XRN1 gene is necessary for the rapid degradation of the SDH1 and SDH2 mRNAs in the presence of glucose
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. SDH function is tailored in different cell types to meet the energy demands, SDH function is differently regulated in distinct cell types. Enzyme regulation can occur via transcription factors, post-transcriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In Brassica hexaploids transcriptions of SDH genes are activated by long non-coding RNAs possibly to stimulate energy production via TCA cycle
physiological function
succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. SDH function is tailored in different cell types to meet the energy demands, SDH function is differently regulated in distinct cell types. Enzyme regulation can occur via transcription factors, post-transcriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview. In human cells, the nuclear respiratory factor-1 (NRF-1) initially is the primary transcriptional regulator of mitochondrial biogenesis. NRF-1 also induces SDH expression through binding to the gene promoters of SDHA and SDHD in the aerobic cardiomyocyte. Low levels of NFR-1 downregulate SDHA and thereby SDH complex expression. This stabilizes HIF-1 and promotes its nuclear translocation and high expression of glucose transporters and heme oxygenase-1. Transcription of the genes encoding SDH subunits (particularly SDHB) of human myoblast cells requires NRF-1 and NRF-2 transcription factors. Certain levels of desuccinylase SIRT5 are required for physiological activity of SDH and any imbalance i.e. either too low or too high levels, may influence SDH activity. Direct effectors are either deactivators such as oxaloacetate or activators such as substrates, anions, reduced quinone, ATP, and reduction. The interaction between SDH and oxaloacetate renders the enzyme inactive, while the interaction between the activator and enzyme prevent such interaction with oxaloacetate
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. SDH function is tailored in different cell types to meet the energy demands, SDH function is differently regulated in distinct cell types. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. SDH function is tailored in different cell types to meet the energy demands, SDH function is differently regulated in distinct cell types. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. SDH function is tailored in different cell types to meet the energy demands, SDH function is differently regulated in distinct cell types. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview
physiological function
succinate:quinone oxidoreductase (SQR) is a multisubunit membrane-associated enzyme found in the cytoplasm of bacteria and in the matrix of mitochondria (where it is commonly termed complex II). The enzyme is central to cellular metabolism and energy conversion, contributing to the tricarboxylic acid cycle and the electron transport chain. It catalyzes the oxidation of succinate to fumarate, which is coupled to electron transfer through flavin adenine dinucleotide (FAD) and three Fe-S clusters, resulting in the reduction of the electron carrier ubiquinone to ubiquinol. Succinate:quinone oxidoreductase (SQR) functions in energy metabolism, coupling the tricarboxylic acid cycle and electron transport chain in bacteria and mitochondria
physiological function
Megalodesulfovibrio gigas
the membrane-embedded quinol:fumarate reductase (QFR) in anaerobic bacteria catalyzes the reduction of fumarate to succinate by quinol in the anaerobic respiratory chain
physiological function
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the enzyme is involved in electron transfer via the respiratory chain
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physiological function
Megalodesulfovibrio gigas DSM 1382
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the membrane-embedded quinol:fumarate reductase (QFR) in anaerobic bacteria catalyzes the reduction of fumarate to succinate by quinol in the anaerobic respiratory chain
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physiological function
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deletion of the sdh1 operon does not yield any growth phenotypes on succinate or other nonfermentable carbon sources
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physiological function
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presence of the Sdh2 operon is essential for growth. Isoform Sdh2 is the generator of the membrane potential under hypoxia
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physiological function
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succinate dehydrogenase (SDH) is a protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, overview
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physiological function
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acetylation can participate in the modulation of the enzymatic activity of SDH, a key enzyme of the tricarboxylic acid cycle, along with the well-known mechanisms of inhibition by oxaloacetic acid, oxidative stress, or mutations in enzyme subunits, in maintaining the energy supply, membrane potential, and other functions of mitochondria
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physiological function
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succinate dehydrogenase (SDH) is a protein complex that links the Krebs cycle to the electron transport system. It can produce significant amounts of superoxide and hydrogen peroxide (H2O2), kinetic mechanism and computational modelling including the major redox centers in the complex, namely FAD, three iron-sulfur clusters, and a transiently bound semiquinone, overview
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physiological function
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succinate:quinone reductase serves as the respiratory complex II
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additional information
enzyme structure-function relationship, overview
additional information
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enzyme structure-function relationship, overview
additional information
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the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
additional information
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the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
additional information
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the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
additional information
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the membrane part of the enzyme is functionally connected to the active site, structure-function relationship, overview
additional information
FrdAR287 is essential for catalytic protonation/deprotonation of fumarate/succinate, an intriguing mechanism for substrate control of capping domain position is via the charge on the dicarboxylate affecting the pKa of FrdAR287. Ligand control of domain position suggests a mechanism for ingress and egress of substrate facilitated by the changes in the locations of active site residues
additional information
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FrdAR287 is essential for catalytic protonation/deprotonation of fumarate/succinate, an intriguing mechanism for substrate control of capping domain position is via the charge on the dicarboxylate affecting the pKa of FrdAR287. Ligand control of domain position suggests a mechanism for ingress and egress of substrate facilitated by the changes in the locations of active site residues
additional information
Megalodesulfovibrio gigas
quinol:fumarate reductase (QFR) is an integral membrane protein with three subunits: a flavoprotein (subunit A), an iron-sulphur protein (subunit B), and a membrane-embedded subunit (subunit C)
additional information
SDH complex structure and assembly, detailed overview. Detailed analysis of some proteins that are required for the assembly of SDH e.g. Tcm62p, Flx1, Sdh6 (in yeast), SDH7 (in yeast), and Sdh5 (in yeast). Tcm62 most likely has a chaperone function for SDH, while Sdh5 plays a role in SDH1 flavination. The current model of complex II (succinate dehydrogenase) assembly: Sdh5 bound to Sdh1 facilitates flavination of Sdh1. Sdh5 is then released, while Sdh8 chaperone binds the flavinated Sdh1 to facilitate the dimerization of Sdh1 and Sdh2. Sdh6 and Sdh7 assist in either insertion or retention of [Fe-S] clusters within Sdh2. Sdh2 then forms a dimer with Sdh1, while Sdh6/Sdh7 and Sdh8 are released from Sdh2 and Sdh1, respectively. The dimer is subsequently integrated into the membrane where Sdh3-Sdh4 dimer containing a heme b is formed. There is not much information regarding the formation of Sdh3-Sdh4 dimer. Role of SDH2 in flavination. SDHAF3 together with SDHAF1 is asserted as factors required for maturation of Sdh2/SDHB
additional information
SDH complex structure and assembly, detailed overview. The SDHA subunit is a flavoprotein containing a covalently bound FAD cofactor and the binding site for dicarboxylates (e.g. succinate). SDHB is an iron-sulfur cluster protein containing three Fe-S clusters. SDHA and SDHB make up the catalytic domain. They extend out into the matrix and constitute the hydrophilic head. SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them. Detailed analysis of some proteins that are required for the assembly of SDH e.g. Tcm62p, Flx1, SDHAF1 or LYRM8, SDHAF3, and SDHAF2. Tcm62 most likely has a chaperone function for SDH. Role of SDHB in flavination. SDHAF3 together with SDHAF1 is asserted as factors required for maturation of Sdh2/SDHB
additional information
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SDH complex structure and assembly, detailed overview. The SDHA subunit is a flavoprotein containing a covalently bound FAD cofactor and the binding site for dicarboxylates (e.g. succinate). SDHB is an iron-sulfur cluster protein containing three Fe-S clusters. SDHA and SDHB make up the catalytic domain. They extend out into the matrix and constitute the hydrophilic head. SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them. Detailed analysis of some proteins that are required for the assembly of SDH e.g. Tcm62p, Flx1, SDHAF1 or LYRM8, SDHAF3, and SDHAF2. Tcm62 most likely has a chaperone function for SDH. Role of SDHB in flavination. SDHAF3 together with SDHAF1 is asserted as factors required for maturation of Sdh2/SDHB
additional information
succinate dehydrogenase (SDH) can produce significant amounts of superoxide and hydrogen peroxide (H2O2), which hinders the development of next-generation antioxidant therapies targeting mitochondria
additional information
succinate dehydrogenase (SDH) can produce significant amounts of superoxide and hydrogen peroxide (H2O2), which hinders the development of next-generation antioxidant therapies targeting mitochondria
additional information
the membrane-anchored SdhF is a subunit of the enzyme complex II (Sdh2). The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Location and interaction of SdhF subunit in Sdh2 protein. Two distal quinone-binding sites with bound quinones are identified, one distal binding site is formed by neighboring subunits of the complex. Major redox centers in the complex are FAD, three iron-sulfur clusters, and a transiently bound semiquinone. The purified recombinant Sdh2 is a functioning complex that couples succinate oxidation to menadione reduction. Enzyme structure analysis, overview
additional information
-
the membrane-anchored SdhF is a subunit of the enzyme complex II (Sdh2). The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Location and interaction of SdhF subunit in Sdh2 protein. Two distal quinone-binding sites with bound quinones are identified, one distal binding site is formed by neighboring subunits of the complex. Major redox centers in the complex are FAD, three iron-sulfur clusters, and a transiently bound semiquinone. The purified recombinant Sdh2 is a functioning complex that couples succinate oxidation to menadione reduction. Enzyme structure analysis, overview
additional information
Megalodesulfovibrio gigas DSM 1382
-
quinol:fumarate reductase (QFR) is an integral membrane protein with three subunits: a flavoprotein (subunit A), an iron-sulphur protein (subunit B), and a membrane-embedded subunit (subunit C)
-
additional information
-
the membrane-anchored SdhF is a subunit of the enzyme complex II (Sdh2). The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Location and interaction of SdhF subunit in Sdh2 protein. Two distal quinone-binding sites with bound quinones are identified, one distal binding site is formed by neighboring subunits of the complex. Major redox centers in the complex are FAD, three iron-sulfur clusters, and a transiently bound semiquinone. The purified recombinant Sdh2 is a functioning complex that couples succinate oxidation to menadione reduction. Enzyme structure analysis, overview
-
additional information
-
the membrane-anchored SdhF is a subunit of the enzyme complex II (Sdh2). The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Location and interaction of SdhF subunit in Sdh2 protein. Two distal quinone-binding sites with bound quinones are identified, one distal binding site is formed by neighboring subunits of the complex. Major redox centers in the complex are FAD, three iron-sulfur clusters, and a transiently bound semiquinone. The purified recombinant Sdh2 is a functioning complex that couples succinate oxidation to menadione reduction. Enzyme structure analysis, overview
-
additional information
-
the membrane part of the enzyme is functionally connected to the active site, structure-function relationship, overview
-
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11000
-
1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
110000 - 114000
-
excluding cytochrome b, calculation from FAD-content and subunit composition
118000
-
calculation from subunit composition
119800
-
monomeric recombinant C-terminally His6-tagged enzyme, gel filtration
12800
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
135000
-
high resolution clear-native electrophoresis
13900
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
14080
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
14300
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
147000
-
calculation from Stokes radius and sedimentation coefficient
150000
-
blue native gel electrophoresis
160000 - 167000
-
including cytochrome b, calculation from FAD-content and subunit composition
16638
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
16675
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
17000
-
1 * 72000 (flavoprotein) + 1* 30000, and 1 * 15000 + 1 * 17000 as membrane anchor (at least one of the latter a cytochrome b-protein), precipitation of protein with specific antibody and SDS-PAGE
170000
-
sedimentation equilibrium centrifugation of preparation containing Triton X-100
18000
-
1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE
180000
-
dimeric form, gel filtration
23000
-
3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
260000
-
Blue-native PAGE
29000
-
3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
29600
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
30229
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
32205
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
35000
-
iron-sulphur subunit
36471
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
37000
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
54000
-
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
60000
-
1 * 60000 + 1* 25000, SDS-PAGE
62000
-
? * 62000 + ? * 26000
63000
x * 63000, SDS-PAGE
63075
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
64000
-
1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE
65600
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
69000
-
fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase
7000
-
1 * 7000 + 1* 27000, SDS-PAGE
70185
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
71000
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE
73000
-
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer
100000
-
gel filtration
100000
-
succinate dehydrogenase
100000
-
SDS-PAGE after cross-linkage with dimethylsuberimidate, sedimentation equilibrium centrifugation
11100
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
11100
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
12000
-
1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
12000
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
120000
-
-
120000
-
larval and adult complex II, non-denaturating PAGE
120000
3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis
120000
-
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
120000
-
3 * 120000, about, wild-type enzyme, SDS-PAGE
120000
-
4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
13000
-
1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE
13000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
13000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
13000
-
fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase
14000
-
1 * 72000, 1 * 28000, 1 * 14000
14000
-
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
14000
x * 67000 + x * 33000 + x * 28000 + x * 14000, SDS-PAGE
15000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
15000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
15000
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE
15000
-
fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase
15000
-
1 * 72000 (flavoprotein) + 1* 30000, and 1 * 15000 + 1 * 17000 as membrane anchor (at least one of the latter a cytochrome b-protein), precipitation of protein with specific antibody and SDS-PAGE
15000
-
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
15300
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
15300
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
200000
-
including cytochrome b, sedimentation equilibrium centrifugation
200000
-
calculated from the molar mass of the enzyme particle and its contents of Triton and phospholipid
25000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
25000
-
enzyme containing cytochrome b, 1 * 79000 + 1 * 31000 + 1 * 25000
25000
-
1 * 79000 + 1 * 31000 + 1 * 25000
26000
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE
26000
-
1 * 65000 + 1 * 26000, large subunit is a flavoprotein, small subunit is an iron-sulfur protein
26000
-
? * 62000 + ? * 26000
27000
-
1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
27000
-
fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase
27000
-
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer
27000
-
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
27097
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
27097
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
28000
-
1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE
28000
-
1 * 72000, 1 * 28000, 1 * 14000
28000
-
1 * 65000 (flavoprotein) + 1 * 28000 (ironprotein) + 19000 (cytochrome protein, membrane anchor), precipitation of radiolabeled protein with specific antibody and SDS-PAGE
28000
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
28000
x * 67000 + x * 33000 + x * 28000 + x * 14000, SDS-PAGE
28064
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
28064
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
28400
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
28400
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
30000
-
sum of molecular weights of membrane anchor subunits is about 30 kDa
30000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
30000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
30000
-
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer
31000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
31000
-
enzyme containing cytochrome b, 1 * 79000 + 1 * 31000 + 1 * 25000
31000
-
1 * 79000 + 1 * 31000 + 1 * 25000
31000
-
1 * 79000 + 1 * 31000, SDS-PAGE
31000
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
32000
-
x * 32000, recombinant SDISP, SDS-PAGE
32000
-
1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE
33000
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
33000
x * 67000 + x * 33000 + x * 28000 + x * 14000, SDS-PAGE
410000
-
PAGE
410000
-
non-denaturing PAGE
500000
-
native PAGE
500000
-
wild-type enzyme, consisting of 360 kDa from protein and an unknown contribution of detergent and lipid, native PAGE
65000
-
1 * 65000 + 1 * 26000, large subunit is a flavoprotein, small subunit is an iron-sulfur protein
65000
-
1 * 65000 (flavoprotein) + 1 * 28000 (ironprotein) + 19000 (cytochrome protein, membrane anchor), precipitation of radiolabeled protein with specific antibody and SDS-PAGE
66000
-
1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
66000
-
x * 70000, about, HA-tagged Sdh1p, SDS-PAGE, x * 66000, cleaved HA-tagged Sdh1p, SDS-PAGE
66000
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
66000
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
67000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
67000
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
67000
-
3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
67000
x * 67000 + x * 33000 + x * 28000 + x * 14000, SDS-PAGE
68000
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
68000
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
70000
-
flavoprotein subunit, identified by Western blot analysis
70000
-
x * 70000, about, HA-tagged Sdh1p, SDS-PAGE, x * 66000, cleaved HA-tagged Sdh1p, SDS-PAGE
70000
x * 70000, flavoprotein of succinate dehydrogenase, SDS-PAGE
70000
-
1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE
72000
-
1 * 72000, 1 * 28000, 1 * 14000
72000
-
1 * 72000 (flavoprotein) + 1* 30000, and 1 * 15000 + 1 * 17000 as membrane anchor (at least one of the latter a cytochrome b-protein), precipitation of protein with specific antibody and SDS-PAGE
73234
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
73234
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
79000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
79000
-
enzyme containing cytochrome b, 1 * 79000 + 1 * 31000 + 1 * 25000
79000
-
1 * 79000 + 1 * 31000 + 1 * 25000
79000
-
1 * 79000 + 1 * 31000, SDS-PAGE
90000 - 100000
-
monomeric form, gel filtration
90000 - 100000
-
soluble enzyme, gel filtration, ultracentrifugation
97000 - 105000
-
sedimentation
97000 - 105000
-
heart, sedimentation, chromatography on agarose, calculation from FAD content
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 67000 + x * 33000 + x * 28000 + x * 14000, SDS-PAGE
?
-
two different stage specific forms of complex II (EC 1.3.5.1) share a comme iron-sulfur subunit
?
-
enzyme consists of a 65000 Da flavoprotein SdhA, a 29000 Da iron-sulfur protein SdhB, and a 19000 Da subunit SdhC containing two b-type cytochromes, SDS-PAGE
?
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
?
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
?
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
?
-
3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
?
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
?
-
? * 62000 + ? * 26000
?
x * 70000, flavoprotein of succinate dehydrogenase, SDS-PAGE
?
-
1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE
?
-
x * 70000, about, HA-tagged Sdh1p, SDS-PAGE, x * 66000, cleaved HA-tagged Sdh1p, SDS-PAGE
?
-
x * 32000, recombinant SDISP, SDS-PAGE
?
-
x * 32000, recombinant SDISP, SDS-PAGE
-
?
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
?
-
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
-
?
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
?
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
-
?
-
complex II is comprised of two hydrophilic proteins, flavoprotein (Fp) and iron-sulfur protein (Ip), and two transmembrane proteins (CybL and CybS), as well as prosthetic groups required for electron transfer from succinate to ubiquinone
dimer
-
1 * 65000 (flavoprotein) + 1 * 28000 (ironprotein) + 19000 (cytochrome protein, membrane anchor), precipitation of radiolabeled protein with specific antibody and SDS-PAGE
dimer
-
amino acid sequence around the flavin site
dimer
-
two additional polypeptides of 14000 and 15000 are necessary for the two large subunits to associate with the membrane
dimer
-
1 * 60000-79000 + 1 * 24000-31000, SDS-PAGE
dimer
-
calculation from gene sequence
dimer
-
1 * 65000 + 1 * 26000, large subunit is a flavoprotein, small subunit is an iron-sulfur protein
dimer
-
1 * 7000 + 1* 27000, SDS-PAGE
dimer
-
1 * 72000 (flavoprotein) + 1* 30000, and 1 * 15000 + 1 * 17000 as membrane anchor (at least one of the latter a cytochrome b-protein), precipitation of protein with specific antibody and SDS-PAGE
dimer
-
biosynthesis and processing
dimer
-
1 * 60000 + 1* 25000, SDS-PAGE
dimer
-
amino acid composition of subunits
dimer
-
biosynthesis and processing
dimer
-
1 * 79000 + 1 * 31000, SDS-PAGE
heterotrimer
determination and analysis of the cryo-electronic microscopy structure of trimeric succinate dehydrogenase with the membrane-anchor SdhF at 2.8 A resolution. The membrane-anchored SdhF is a subunit of the enzyme complex II. The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Within the trimer, each of the three assemblies contains four canonical proteins: an FAD (flavin adenine dinucleotide)-binding protein (SdhA), an iron-sulfur protein (SdhB), and two membrane-anchored proteins (SdhC and SdhD), each with three transmembrane helices
heterotrimer
-
determination and analysis of the cryo-electronic microscopy structure of trimeric succinate dehydrogenase with the membrane-anchor SdhF at 2.8 A resolution. The membrane-anchored SdhF is a subunit of the enzyme complex II. The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Within the trimer, each of the three assemblies contains four canonical proteins: an FAD (flavin adenine dinucleotide)-binding protein (SdhA), an iron-sulfur protein (SdhB), and two membrane-anchored proteins (SdhC and SdhD), each with three transmembrane helices
-
heterotrimer
-
determination and analysis of the cryo-electronic microscopy structure of trimeric succinate dehydrogenase with the membrane-anchor SdhF at 2.8 A resolution. The membrane-anchored SdhF is a subunit of the enzyme complex II. The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Within the trimer, each of the three assemblies contains four canonical proteins: an FAD (flavin adenine dinucleotide)-binding protein (SdhA), an iron-sulfur protein (SdhB), and two membrane-anchored proteins (SdhC and SdhD), each with three transmembrane helices
-
homodimer
Megalodesulfovibrio gigas
QFR is a homodimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme bL in the hydrophobic subunit C. Two heterotrimeric complexes, each comprising subunits A, B and C, form one stable homodimer (A2B2C2) with major contacts between two C subunit. The formation of the homo-dimer, (A2B2C2), arises from contact of the two C subunits
homodimer
Megalodesulfovibrio gigas DSM 1382
-
QFR is a homodimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme bL in the hydrophobic subunit C. Two heterotrimeric complexes, each comprising subunits A, B and C, form one stable homodimer (A2B2C2) with major contacts between two C subunit. The formation of the homo-dimer, (A2B2C2), arises from contact of the two C subunits
-
monomer
-
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
monomer
-
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
-
oligomer
-
homodimeric complex of heterotrimers of A, B, and C subunits
oligomer
-
homodimeric complex of heterotrimers of A, B, and C subunits
oligomer
-
homodimeric complex of heterotrimers of A, B, and C subunits
tetramer
-
the enzyme complex consits of four subunits: a flavoprotein SDH1, an iron-sulfur protein SDH2, two integral membrane subunits SDH3 and SDH4. Protein SDHA F2 is needed for assembly and activity of SDH and also for normal root elongation
tetramer
-
1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
tetramer
QFR is composed of Fp, Ip, CybL and CybS subunits
tetramer
-
heart, succinate dehydrogenase, SDS-PAGE
tetramer
-
amino acid sequence of Ip subunit
tetramer
-
1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE
tetramer
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE
tetramer
-
fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase
tetramer
-
secondary structure
tetramer
enzyme QFR is composed of four polypeptide chains, two of which are soluble (flavoprotein, FrdA and iron-sulfur protein, FrdB) and two of which are membrane-spanning (FrdC and FrdD)
tetramer
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
tetramer
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
tetramer
-
determined by high resolution clear-native electrophoresis and Western blot analysis. Enzyme consists of four subunits: a flavoprotein subunit (Fp, SDH1) and an iron-sulphur subunit (Ip, SDH2) form a soluble heterodimer, which binds to a membrane anchor b-type cytochrome (SDH3)/CybS (SDH4) heterodimer
tetramer
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
tetramer
-
composed of a catalytic dimer, comprising a flavoprotein subunit Sdh1p and an iron-sulfur protein Sdh2p, and a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
tetramer
-
subunits SdhA, SdhB, SdhC, and SdhD
tetramer
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
tetramer
-
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
-
tetramer
-
4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
tetramer
-
4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
-
tetramer
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
tetramer
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
trimer
-
homotrimeric complex of the heterotrimeric protomer
trimer
-
trimer of the heterotrimeric protomer. 67000, subunit SdhA, 29000, subunit SdhB, 23000, subunit SdhC, SDS-PAGE
trimer
-
1 * 65000-68700, Fp-subunit, FAD-binding, 1 * 27500-28000, Ip-subunit, Fe-S cluster containing, 1 * 19000-22000, membrane binding and cytochrome b containing subunit, SDS-PAGE
trimer
3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis
trimer
-
1 * 72000, 1 * 28000, 1 * 14000
trimer
-
1 * 72000, 1 * 28000, 1 * 14000
-
trimer
-
3 * 120000, about, wild-type enzyme, SDS-PAGE
trimer
-
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
trimer
-
3 * 120000, about, wild-type enzyme, SDS-PAGE
-
trimer
-
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
-
trimer
-
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer
trimer
-
enzyme containing cytochrome b, 1 * 79000 + 1 * 31000 + 1 * 25000
trimer
-
1 * 79000 + 1 * 31000 + 1 * 25000
additional information
-
SdhC and SdhD form an active complex
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
it is shown that lung stage L3 larvae mitochondria contain larval flavoprotein subunit (Fp) and adult flavoprotein subunit at a ratio of 1:0.56, and that most lung stage L3 larvae cytochrome b containing subunits CybS are of the adult form. This clearly indicates that the rearrangement of complex II begins with a change in the isoform of the anchor CybS subunit, followed by a similar change in the Fp subunit
additional information
the enzyme structure comprises four subunits and five co-factors, subunit structure comparisons, overview
additional information
-
the enzyme structure comprises four subunits and five co-factors, subunit structure comparisons, overview
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
the enzyme from Bacillus subtilis consists of two hydrophilic protein subunits comprising succinate dehydrogenase, and a di-heme membrane anchor protein harboring two putative quinone binding sites, overview
additional information
-
the enzyme from Bacillus subtilis consists of two hydrophilic protein subunits comprising succinate dehydrogenase, and a di-heme membrane anchor protein harboring two putative quinone binding sites, overview
-
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
cf. EC 1.3.5.1, both complexes contain a catalytic domain, composed of a subunit with a covalently bound flavin cofactor, the dicarboxlyate binding site, and an iron-sulfur subunit, which contains three distince iron-sulfur clusters. The catalytic domain is bound to the cytoplasmic membrane by two hydrophobic membrane anchor subunits that also form the sites for interaction with quinones. The catalytic domain is highly conserved and reflect the biochemical and structural similarity of EC 1.3.5.1 (SQR) and 1.3.5.4 (QFR). SQR, in addition to differences in the type of quinones it uses as compared to QFR, is known to contain a single B556 heme moiety, showing to have bis-histidine axial ligation
additional information
cf. EC 1.3.5.1, both complexes contain a catalytic domain, composed of a subunit with a covalently bound flavin cofactor, the dicarboxlyate binding site, and an iron-sulfur subunit, which contains three distince iron-sulfur clusters. The catalytic domain is bound to the cytoplasmic membrane by two hydrophobic membrane anchor subunits that also form the sites for interaction with quinones. The catalytic domain is highly conserved and reflect the biochemical and structural similarity of EC 1.3.5.1 (SQR) and 1.3.5.4 (QFR). SQR, in addition to differences in the type of quinones it uses as compared to QFR, is known to contain a single B556 heme moiety, showing to have bis-histidine axial ligation
additional information
succinate:quinone oxidoreductase (SQR) is a multisubunit membrane-associated enzyme. The structure of SdhA is composed of four domains: an FAD-binding domain (residues 1-245 and 351-431), which includes a Rossmann-type fold and provides the binding site for FAD, a capping domain composed of residues 245-351, a helical domain composed of residues 431-547, and a C-terminal domain composed of residues 547-583. The position of the SdhA capping domain is markedly different in the SdhAE assembly relative to SQR, structure comparisons, proposed SdhA assembly pathway, detailed overview. In contrast to the significant structural rearrangements in SdhA, which accompany formation of the SdhAE complex, the structure of SdhE is virtually unchanged
additional information
facultative anaerobic bacterium
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
structure-function relationships of SDH based on the porcine heart enzyme crystal structure, modeling at 2.4 A resolution, PDB ID 1ZOY
additional information
-
the catalytic core SdhA and SdhB subunits contain the redox cofactors that participate in electron transfer to ubiquinone. Sdh1 contains the covalently bound FAD cofactor and the binding site for succinate. Sdh2 contains the three Fe-S centers that mediate electron transfer to ubiquinone in the complex of succinate-ubiquinone dehydrogenase, EC 1.3.5.1, regulation of SDH, overview.The membrane domain consists of two subunits SdhC and SdhD. The membrane domain contains a bound heme b moiety at the subunit interface with SdhC and SdhD each providing one of the two axial His ligands
additional information
SDH complex structure and assembly, detailed overview. Succinate dehydrogenase in eukaryotes is composed of four subunits SDHA-D (human). The SDHA subunit is a flavoprotein containing a covalently bound FAD cofactor and the binding site for dicarboxylates (e.g. succinate). SDHB is an iron-sulfur cluster protein containing three Fe-S clusters. SDHA and SDHB make up the catalytic domain. They extend out into the matrix and constitute the hydrophilic head. SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them. SDHB is sandwiched between SDHA on the matrix side, and SDHC and SDHD in the membrane. These two transmembrane subunits thus form the hydrophobic anchor. A small patch of the anchor is exposed on the distal side, to the aqueous intermembrane space. Therefore, the structure of SDH can be divided into two main modules: SDHA and SDHB as the membrane extrinsic (soluble) domain, and SDHC and SDHD as the membrane domain. The interface between the catalytic head domain and the anchor subunits can be separated without the use of detergent, making the catalytic domain an extrinsic membrane protein
additional information
-
SDH complex structure and assembly, detailed overview. Succinate dehydrogenase in eukaryotes is composed of four subunits SDHA-D (human). The SDHA subunit is a flavoprotein containing a covalently bound FAD cofactor and the binding site for dicarboxylates (e.g. succinate). SDHB is an iron-sulfur cluster protein containing three Fe-S clusters. SDHA and SDHB make up the catalytic domain. They extend out into the matrix and constitute the hydrophilic head. SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them. SDHB is sandwiched between SDHA on the matrix side, and SDHC and SDHD in the membrane. These two transmembrane subunits thus form the hydrophobic anchor. A small patch of the anchor is exposed on the distal side, to the aqueous intermembrane space. Therefore, the structure of SDH can be divided into two main modules: SDHA and SDHB as the membrane extrinsic (soluble) domain, and SDHC and SDHD as the membrane domain. The interface between the catalytic head domain and the anchor subunits can be separated without the use of detergent, making the catalytic domain an extrinsic membrane protein
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
structure molecular dynamic simulations using the crystal structure with PDB ID 1PB4
additional information
SDH complex structure and assembly, detailed overview. Succinate dehydrogenase in eukaryotes is composed of four subunits SDH1-4
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
the enzyme is part of the tetrameric succinate dehydrogenase complex
additional information
-
the enzyme is part of the tetrameric succinate dehydrogenase complex
-
additional information
-
SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
additional information
-
SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
-
additional information
-
SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
-
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
-
circular dichroism and blue-native polyacrylamide gel electrophoresis reveal that the enzyme forms a trimer with a predominantly helical fold, overview
additional information
-
circular dichroism and blue-native polyacrylamide gel electrophoresis reveal that the enzyme forms a trimer with a predominantly helical fold, overview
-
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
additional information
succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
additional information
-
succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
-
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H277R
-
the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
H277Y
-
the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
G168D
-
enzyme not assembled, properties of heme bP and heme bD seem normal
H113L
-
enzyme not assembled
H113M
-
assembled enzyme, low enzyme activity, altered properties of heme bD compared to wild-type
H113Y
-
enzyme not assembled, contains heme
H13Y
-
assembles enzyme with about 50% of normal activity, alters properties of heme bP and heme bD compared to wild-type, the isolated enzyme is not stable in the presence of succinate
H155L
-
assembled enzyme, the enzyme has some activity but apparently is unstable
H155Y
-
enzyme not assembled, contains heme
H28L
-
assembles succinate dehydrogenase, active succinate dehydrogenase but inactive succinate: quinone reductase, contains heme bP but lacks low potential heme
H28Y
-
enzyme not assembled, contains heme
H47Y
-
assembles fully active enzyme
H70L
-
enzyme not assembled
H70Y
-
enzyme not assembled
H70Y/Y73S
-
assembled enzyme, enzyme activity is 30% of normal
S214C/Q215G
-
substitution in the IP subunit, mutant is enzymatically impaired and less stable than wild-type
P211F
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211H
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211L
mutant shows the weakest SDH activity, mutant shows a significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate in P211L mutant is increased compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211N
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211Q
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211R
mutant shows significant reduced SDH activity, life span of mutant is not reduced compared to wild-type, embryogenesis is impaired in mutant, in P211R mutant are twice as many dead embryos compared to wild-type (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
C247
-
mutation in flavoprotein subunit FrdA. Increase in fumarate reduction rate, slight increase in succinate oxidation. Residue C247 of FrdA is responsible for the N-ethylmaleimide sensitivity shown by fumarate reductase but is not required for catalytic activity or the tight-binding of oxalacetate
D288N
site-directed mutagenesis, the FrdAD288N variant shows minimal residual fluorescence, suggesting covalent flavinylation is severely compromised
D95E
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
D95L
-
site-directed mutagenesis of subunit C, the mutant shows a shifted pH-optimum but similar activity compared to the wild-type enzyme
E101D
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
E101L
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
E245Q
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation. Mutant crystal structure analysis, overview
E49A
decrease in catalytic efficiency of both fumarate reduction and succinate oxidation
E49Q
decrease in catalytic efficiency of both fumarate reduction and succinate oxidation
F20L
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Phe-20 is not involved in the Q binding
G227L
-
site-directed mutagenesis of subunit B, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
G227L/D95E
-
site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0
G227L/D95L
-
site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0
H232S
-
mutation in flavoprotein subunit FrdA. Decrease in fumarate reduction, strong decrease in succinate oxidation. Residue H232 is the general acid-base catalyst
H30A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, His-30 is not involved in the Q binding
H355S
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
H44C
-
the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 38% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H44R
-
the mutation does not allow cells to grow anaerobically on glycerol and fumarate, the substitution produces an inactive complex
H44S
-
the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 32% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H44Y
-
the mutation allows cell growth in glycerol/fumarate medium at a 7fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 17% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H71C
-
role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Mutant H71C results in a protein that retains penta-coordinated heme b indicating that Cys is not able to provide coordination for the heme in Escherichia coli SQR even in its optimal structural position. Km (ubiquinone): 0.012 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. Mutant H71C retains 43% of ubiquinone reductase activity compared to wild-type SQR, quinone reductase activity is impaired to a greater extent than its succinate-oxidase activity measured with phenazine ethosulfate
H71L
-
mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme
H71Q
-
mutation in SdhC subunit, 82% and 69% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively
H71Y
-
mutant lacks heme. Km (ubiquinone): 0.01 mM compared to 0.0025 mM wild-type, lower ubiquinone or phenazine ethosulfate reductase activity compared to mutant H71C or double mutant H71Y/A72C
H71Y/A72C
-
role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Double mutant assembles within the membrane but without heme, and it retains the ability to reduce quinone. Km (ubiquinone): 0.013 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. The Y71C72 double mutant shows significant improvement in its activity compared to H71Y or H71C
H82R
-
menaquinone, ubiquinone and b-type cytochrome levels are present in normal amounts, the mutation alters the electron transfer properties of the iron-sulfur and flavin redox centers of the catalytic domain, functional electron flow from 2,3-dimethyl-1,4-naphthoquinone or from the electron transport chain is impaired, the mutant can be reduced normally by single-electron donors such as benzyl viologen
H84L
-
mutation in SdhC subunit, 54% and 23% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively
H91L
-
mutant enzyme produces more superoxide than the wild-type enzyme
I150E
-
mutation lowers the midpoint potential of the [4Fe-4S] cluster
I150H
-
mutation lowers the midpoint potential of the [4Fe-4S] cluster
I28E
-
mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme
L220S
-
mutation does not alter the redox behavior of the [4Fe-4S] cluster but instead lowers the midpoint potential of the [3Fe-4S] cluster
Q78L
-
site-directed mutagenesis of subunit D, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
R19A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Arg-19 is not involved in the Q binding
R248H
-
mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation
R248L
-
mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation
R287K
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
R28E/E29I
mutation in subunit FrdC, retains normal level of activity
R28L
mutation in subunit FrdC, retains normal level of activity
R28L/E9L
mutation in subunit FrdC, retains normal level of activity
R28L/R81A
mutation in subunits FrdC/FrdD, loss of activtiy with ubiquinone and menaquinol
R28N
mutation in subunit FrdC, retains normal level of activity
R31A
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Arg-31 is a critical residue for succinate-Q-reductase
R31H
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity
R31K
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity, it occupies a much larger space than the primary amine of lysine, extends a longer distance, and may provide more chance for hydrogen bond formation, it may stabilize Q binding through pi-pi interactions between the guanidino group and the benzoquinone ring
R390K
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
R390Q
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
R81A
mutation in subunit FrdD, retains normal level of activity
R81E
mutation in subunit FrdD, retains normal level of activity
R81K
mutation in subunit FrdD, retains normal level of activity
S27A
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Ser-27 is a critical residue for succinate-Q-reductase, it participates in a hydrogen bond at the Q-binding site of the C subunit
S27C
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding
S27T
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding
S33A
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 35% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase, the mutation of Ser-33 to alanine may greatly reduce enzyme turnover without affecting the affinity for Q
S33C
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 44% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase
S33T
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 88% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase
T17A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Thr-17 is not involved in the Q binding
T23A
-
the mutation yields cells capable of aerobic growth on M9/succinate medium at a rate slightly slower than that of complement strain, 40% decrease in the specific activity of the mutant to catalyze electron transfer from succinate to Q, apparent Km for Q2 is the same as that of complement reductase, Thr-23 may not be involved in Q binding
A3G
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
C191Y
-
a novel germline missense SDHB mutation (C191Y) in a patient affected by a glomus tumor is reported. The missense mutation hits an amino acid residue conserved from mammals to the yeast Saccharomyces cerevisiae. Histochemistry demonstrates that SDH activity is selectively absent in the patient tumor tissue
G12S
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
G148D
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
H145N
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
H50R
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
L157X
-
the case of a novel SDHB mutation (L157X) in a Japanese patient with abdominal paraganglioma following malignant lung metastasis is reported. Novel mutation is a nonsense mutation, resulting in a truncated protein. In addition, an asymptomatic carrier of the SDHB mutation in this family is identified
L85X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
R17X
-
naturally occuring mutation in the SDHD gene of a 29-year-old man showing metastases in both lungs and the liver, but no increased hormone production by the tumor, phenotype, overview
R46Q
-
a naturally occuring mutation in gene SDHB in a Japanese family with both abdominal and thoracic paraganglioma following metastasis
R46X
-
naturally ocurring mutations, the recurrent stop-codon mutation in succinate dehydrogenase subunit B gene might play a role in cellular pre-adaptation to hypoxia in normal peripheral blood and childhood T-cell acute leukemia, overview
S163P
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
W61X
-
an unusual naturally occurring SDHC gene non-sense mutation in a case of laryngeal paraganglioma, phenotype with an additional thyroid papillary carcinoma, overview
Y114X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
H243L
an amino-acid substitution of a highly conserved histidine residue within the third cysteine-rich cluster of SdhB replaced by a leucine residue confers carboxin resistance to the organism
B89G
-
succinate dehydrogenase D polypeptide, the mutation conferrs resistance to carboxin but not to thenoyltrifluoroacetone
C184Y
-
SDH2C184Y mutant allele equivalent to human SDHBC191Y does not restore the OXPHOS phenotype of the DELTAsdh2 null mutant. In the C184Y mutant, SDH activity is abolished along with a reduction in respiration. Sensitivity to oxidative stress is increased in the mutant, as revealed by reduced growth in the presence of menadione. The frequency of petite colony formation is increased in the C184Y mutant, indicating an increased mtDNA mutability
C630A/R638A
-
naturally occuring mutant, overexpression of Sdh5 partially does not restore growth of the double mutant
C78A/H106A
-
site-directed mutagenesis of the subunits Sdh3p and Sdh4p, leads to highly reduced to undetectable levels of heme b562 and reduced cell growth compared to the wild-type enzyme
C78H
-
mutation in Sdh4 subunit, 53% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
C85A
-
mutation in Sdh4 subunit, 94% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
D117V
-
reduced covalent FAD content
D88E
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
D88K
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity and FAD content
D88N
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity and FAD content, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
F103V
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Phe-103 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase, the enzyme is thermolabile at temperatures above 25°C
F69V
-
mutation in anchor subunit Sdh4, 56% of wild-type kcat
G70V/R638A
-
naturally occuring Sdh1 mutant, the mutant shows slightly reduced growth without glucose
H106L/D117V
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25°C
H106Y
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, the quinone reductase activity is not greatly impaired, the enzyme is thermolabile at temperatures above 25°C
H113A
-
mutation in Sdh3 subunit, 61% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H113Q
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, His-113 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase
H30A
-
mutation in Sdh3 subunit, 97% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H37A
-
mutation in Sdh4 subunit, 100% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H46A
-
mutation in Sdh3 subunit, 45% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H46D
-
mutation in Sdh3 subunit, 47% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H84A
-
mutation in Sdh3 subunit, 97% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H99A
-
mutation in Sdh4 subunit, 75% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
K132E
-
mutation in Sdh4 subunit affects heme assembly
K132G
-
mutation in Sdh4 subunit affects heme assembly
K132Q
-
mutation in Sdh4 subunit, reduced heme content
K132V
-
mutation in Sdh4 subunit affects heme assembly
L122stop
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25°C
P190Q
-
mutation in Sdh2 subunit, mutants have reduced succinate-ubiquinone oxidoreductase activity and are hypersensitive to oxygen and paraquat
R47C
-
site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity
R47E
-
site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity and FAD content
R47K
-
site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
R582A
-
site-directed mutagenesis, inactive mutant, no growth without glucose
R582A/M599R
-
the mutant shows slightly reduced growth without glucose
R582C
-
site-directed mutagenesis, the mutant shows slightly reduced growth without glucose
R638A
-
naturally occuring mutant, the mutant shows highly reduced growth without glucose, overexpression of Sdh5 partially restores growth of the single R638A mutant
S71A
-
mutation in anchor subunit Sdh4, 43% of wild-type kcat
S94E
-
mutation in Sdh4 subunit, mutants have reduced succinate-ubiquinone oxidoreductase activity and are hypersensitive to oxygen and paraquat
W116R
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Trp-116 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase
Y89OCH
-
substitution with stop codon truncates Sdh4 by removing the third predicted transmembrane segment, 22% of wild-type activity
E180Q
-
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
E66Q
-
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
H44E
-
site-diirected mutagenesis, although the H44E variant enzyme retains both heme groups, it is unable to catalyze quinol oxidation, the mutant catalyzes the electron transfer from succinate to methylene blue, with reduced activity compared to the wild-type enzyme but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
E29F
-
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione, the succinate-ubiquinone reductase reaction remains unaffected. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
E29F
-
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
E29L
-
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione, the succinate-ubiquinone reductase reaction remains unaffected. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
E29L
-
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
E29L
mutation in subunit FrdC, alters hydrogen bonding to menaquinone
K228L
-
mutation in subunit FrdB. Residue K228 provides a strong hydrogen bond to menaquinone and is essential for reactions with both menaquinone and ubiquinone
K228L
-
mutation in subunit FrdB. Residue K228 provides a strong hydrogen bond to menaquinone and is essential for reactions with both ubiquinone and menaquinone
K228R
-
mutation in subunit FrdB. Residue K228 provides a strong hydrogen bond to menaquinone and is essential for reactions with both menaquinone and ubiquinone
K228R
-
mutation in subunit FrdB. Residue K228 provides a strong hydrogen bond to menaquinone and is essential for reactions with both ubiquinone and menaquinone
D92Y
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
D92Y
-
the naturally occurring mutation of gene SDHD encoding subunit Sdh4p is involved in development of malignant paragangliomas with paraganglioma bone metastases, intrathoracic paraganglioma with lymph node metastases, locally invasive head-and-neck paraganglioma with destruction of the petrosal bone, and locally invasive paraganglioma of the bladder with lymph node metastases, phenotypes, overview
W43X
-
a naturally occurring mutation of the enzyme leads to hypermethylation of the seventh CTCF binding site in the germline and causes paragnaglioma after maternal transmission, study of a three-generation comprising mutation in the germline, phenotype and molecular analysis, overview
W43X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
C78A
-
mutation in Sdh4 subunit, 94% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
C78A
-
site-directed mutagenesis of the subunit Sdh4p residue an axial ligand of heme binding, leads to highly reduced to undetectable levels of heme b562 compared to the wild-type enzyme
H106A
-
mutation in Sdh3 subunit, 78% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H106A
-
site-directed mutagenesis of the subunit Sdh3p residue, an axial ligand of heme binding, leads to highly reduced to undetectable levels of heme b562 compared to the wild-type enzyme
H99L
-
mutation in anchor subunit Sdh4, 29% of wild-type kcat
H99L
-
reduced covalent FAD content
R582W
-
naturally occuring mutant, inactive Sdh1 mutant
R582W
-
site-directed mutagenesis, inactive mutant, no growth without glucose
A86H
-
FAD is non-covalently attached to SdhA. This is prooved by mutant A86H: in contrast to wild-tpye mutant A86H shows an additional fluorescent band which can be detected after SDS-PAGE
A86H
-
in wild-type enzyme FAD is non-covalenly-bound. In the enzyme containing a mutant A86H flavoprotein subunit the FAD is covalently bound
H229Y
the single amino acid substitution in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, the mutant is insensitive to the fungicide
H229Y
-
the single amino acid substitution in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, the mutant is insensitive to the fungicide
-
additional information
-
His44 mutant contains non-covalently bound FAD and loose the ability to oxidize succinate
additional information
His44 mutant contains non-covalently bound FAD and loose the ability to oxidize succinate
additional information
investigation on the role of the amino acid side chain in enzymes with Glu/Gln/Ala substitutions at fumarate reductase FrdA Glu49 and succinate dehydrogenase SdhA, EC 1.5.3.1, Gln50. The mutant enzymes with Ala substitutions in either Frd or Sdh remain functionally similar to their wild type counterparts. There are, however, dramatic changes in the catalytic properties when Glu and Gln are exchanged for each other in Frd and Sdh. Both enzymes are more efficient succinate oxidases when Gln is in the target position and a better fumarate reductase when Glu is present. Structural and catalytic analyses of the FrdA E49Q and SdhA Q50E mutants suggest that coulombic effects and the electronic state of the FAD are critical in dictating the preferred directionality of the succinate/fumarate interconversions
additional information
-
investigation on the role of the amino acid side chain in enzymes with Glu/Gln/Ala substitutions at fumarate reductase FrdA Glu49 and succinate dehydrogenase SdhA, EC 1.5.3.1, Gln50. The mutant enzymes with Ala substitutions in either Frd or Sdh remain functionally similar to their wild type counterparts. There are, however, dramatic changes in the catalytic properties when Glu and Gln are exchanged for each other in Frd and Sdh. Both enzymes are more efficient succinate oxidases when Gln is in the target position and a better fumarate reductase when Glu is present. Structural and catalytic analyses of the FrdA E49Q and SdhA Q50E mutants suggest that coulombic effects and the electronic state of the FAD are critical in dictating the preferred directionality of the succinate/fumarate interconversions
additional information
-
isolation of a mutant in the frdD gene encoding the hydrophic subunit of the fumarate reductase complex. In this mutant, fumarate reductase is not as tightly bound to the membrane. The mutation in the FrdD peptide causes an almost total loss of the ability of the enzyme to oxidize either menaquinol-6, or reduced benzyl viologen. The mutation does not impair the ability of the membrane-bound fumarate reductase complex to function with succinate as substrate
additional information
circular dichroism spectroscopy of wild-type and variant FrdA subunits, measurement of flavin in wild-type and variant FrdA subunits and determination of the quantity of flavin covalently associated with FrdA, overview
additional information
-
circular dichroism spectroscopy of wild-type and variant FrdA subunits, measurement of flavin in wild-type and variant FrdA subunits and determination of the quantity of flavin covalently associated with FrdA, overview
additional information
-
clinical and molecular genetics of patients with the Carney-Stratakis syndrome and germline mutations of the genes coding for the succinate dehydrogenase subunits SDHB, SDHC, and SDHD, causing gastrointestinal stromal tumors, phenotypes, overview
additional information
-
clinical manifestations of familial paraganglioma and phaeochromocytomas, that may include papillary renal cell carcinoma and macrovascular disease, in succinate dehydrogenase B gene mutation carriers, SDH-B mutation carriers develop disease early and predominantly in extra-adrenal locations, disease penetrance is incomplete, phenoypes, overview
additional information
-
determination of distinct heterozygous SDHB missense DNA mutations, the mutational mechanism targeting SDHB is operational in T-cell acute leukemia, overview
additional information
-
germline mutations and variants in the succinate dehydrogenase gene SDHD, encoding the subunit D, in Cowden and Cowden-like syndromes, overview, mutations of the SDH genes can cause diverse pathologies, overview
additional information
-
germline mutations of the SDHB gene are correlated to an elevated risk of malignant, extradrenal tumor development, overview
additional information
-
high frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain, determiunation of sequence variants, overview, mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations, genotype-phenotype correlations, overview
additional information
-
inactivation of SDHD by scrambled and SDHD-targeting small interfering RNA short hairpins, Sc and Di3, expression, succinate dehydrogenase-deficient cells show cell-permeating alpha-ketoglutarate derivatives alleviate pseudohypoxia, overview
additional information
-
mutations of genes SDHb and SDHDencoding subunits of SDH are involved in development of carcinoid tumours and bilateral phaeochromocytoma, phenotype, overview
additional information
-
single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, especially mutation c.456+32G>A of gene SDHA showing significant genotype association with impairment of sperm production, overview
additional information
single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, especially mutation c.456+32G>A of gene SDHA showing significant genotype association with impairment of sperm production, overview
additional information
single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, especially mutation c.456+32G>A of gene SDHA showing significant genotype association with impairment of sperm production, overview
additional information
-
single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, overview
additional information
single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, overview
additional information
single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, overview
additional information
-
splicing defect mutant IVS2+5GA is a naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
additional information
-
construction of a gene SDH3 disruption mutant by gene replacement, effects of mutations of the enzyme subunits on the electron transfer activities in mitochondrial membranes of mutant yeast cells compared to the wild-type strain, overview
additional information
-
the amount of Sdh1p decreases in an FAD transporter flx1D mutant strain, SDH1 coding sequence and the regulatory sequences located downstream of the SDH1 coding region, as well as protein import and cofactor attachment, seem to be not involved in the decrease in the amount of protein, FLX1 deletion or mutation results in a respiration-deficient phenotype, in which the activities of the mitochondrial FAD dependent-enzymes, lipoamide dehydrogenase and succinate dehydrogenase, are reduced, overview
additional information
-
ubiquinone-binding site mutations in the succinate dehydrogenase generate superoxide and lead to the accumulation of succinate
additional information
-
construction of several SDH subunit deletion strains, overview. Truncation of its last 13 residues of sdh1 abrogates this heme binding and renders the cells respiratory defective. Mutation of Arg638 compromises SDH function only when present in combination with a Cys630 substitution. Mutations of either Arg582 or Arg638/Cys630 do not markedly destabilize the Sdh1 polypeptide. The steady-state level of Sdh5 is markedly attenuated in the Sdh1 mutant cells
additional information
expression of a fragment of the Sl SDH2-2 gene encoding the iron sulfur subunit of the succinate dehydrogenase protein complex in the antisense orientation under the control of the 35S promoter leads to an enhanced rate of photosynthesis. When the Sl SDH2-2 gene is repressed by antisense RNA in a guard cell-specific manner, changes in neither stomatal aperture nor photosynthesis are observed. Antisense SDH transgenic tomato plants exhibit elevated aerial growth and fruit yield, growth phenotype, overview
additional information
-
expression of a fragment of the Sl SDH2-2 gene encoding the iron sulfur subunit of the succinate dehydrogenase protein complex in the antisense orientation under the control of the 35S promoter leads to an enhanced rate of photosynthesis. When the Sl SDH2-2 gene is repressed by antisense RNA in a guard cell-specific manner, changes in neither stomatal aperture nor photosynthesis are observed. Antisense SDH transgenic tomato plants exhibit elevated aerial growth and fruit yield, growth phenotype, overview
additional information
-
construction of a sdhCAB deletion mutant DELTAsdh
additional information
-
construction of a sdhCAB deletion mutant DELTAsdh
-
additional information
-
construction of a sdhCAB deletion mutant DELTAsdh
-
additional information
several resistant mutant strains, the SDH activity of mutant strain XRUVI is clearly lower than that of wild-type strain ZJ173 in the absence of amicarthiazol, overview
additional information
several resistant mutant strains, the SDH activity of mutant strain XRUVI is clearly lower than that of wild-type strain ZJ173 in the absence of amicarthiazol, overview
additional information
-
several resistant mutant strains, the SDH activity of mutant strain XRUVI is clearly lower than that of wild-type strain ZJ173 in the absence of amicarthiazol, overview
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