Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + electron donor
succinate + oxidized donor
fumarate + menaquinol
succinate + menaquinone
-
fumarate reductase acts as part of an anaerobic respiratory chain
-
-
r
fumarate + quinol
succinate + ubiquinone
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 + 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
succinate + electron acceptor
fumarate + reduced acceptor
succinate + FAD
fumarate + FADH2
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 + menadione
fumarate + menadiol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + menaquinone
fumarate + menaquinol
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 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 + 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:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
-
-
r
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 + 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 + 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 + 2,3-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
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
A0QPJ1; A0QPJ2; A0QPJ3; A0QPJ4; A0QPJ5;, A0QT07; A0QT08; A0QT09; A0QT10; -
-
-
ir
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
A0QPJ1; A0QPJ2; A0QPJ3; A0QPJ4; A0QPJ5;, A0QT07; A0QT08; A0QT09; A0QT10; -
-
-
ir
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 + duroquinone

fumarate + duroquinol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + duroquinone
fumarate + duroquinol
-
with 2,6-dichlorophenolindophenol
-
-
?
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 + ferrocyanide

fumarate + ferricyanide
-
-
-
-
?
succinate + ferrocyanide
fumarate + ferricyanide
-
-
-
-
?
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-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
-
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
-
with 2,6-dichlorophenolindophenol, best substrate
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
with 2,6-dichlorophenolindophenol, best substrate
-
-
?
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 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
-
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
-
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
-
-
-
-
?
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 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
?
-
-
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 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
fumarate + menaquinol
succinate + menaquinone
-
fumarate reductase acts as part of an anaerobic respiratory chain
-
-
r
fumarate + reduced acceptor
succinate + acceptor
succinate + acceptor
fumarate + reduced acceptor
succinate + caldariellaquinone
fumarate + caldariellaquinol
succinate + electron acceptor
fumarate + reduced acceptor
-
active in aerobic respiration, repressed during anaerobic respiration
-
-
?
succinate + FAD
fumarate + FADH2
succinate + menaquinone
fumarate + menaquinol
succinate + ubiquinone
fumarate + ubiquinol
additional information
?
-
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
succinate + acceptor

fumarate + reduced acceptor
Q8LB02, Q8LBZ7
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
-
-
-
?
succinate + caldariellaquinone

fumarate + caldariellaquinol
O73937 and O73937 and O73939 and O73940
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
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
Q6DLZ2, Q6DLZ3
-
-
-
?
succinate + FAD
fumarate + FADH2
Q6DLZ2, Q6DLZ3
-
-
-
?
succinate + menaquinone

fumarate + menaquinol
-
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
-
-
-
-
?
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
-
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
-
-
-
-
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
P0AC41
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
r
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
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
P21912, Q99643
-
-
-
?
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
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
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
-
-
-
r
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
?
-
-
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
?
-
-
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
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-methoxy-5-methylphenazinium methyl sulfate
-
-
2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
-
-
2,6-dichlorophenolindophenol
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
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
Plumbagin
-
a quinone analogue
quinone
-
with a periplasmically oriented quinone binding site of the enzyme
2,6-dichlorophenolindophenol

-
-
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
in presence of phenazine methosulfate
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
-
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
-
4.5-5 nmol cytochrome b per mg protein; cytochrome b-557.5
-
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
-
1 mol per mol of succinate dehydrogenase
-
cytochrome b
-
the isolated two-subunit membrane anchoring protein contains 35 nmol cytochrome b-556 per mg protein
-
cytochrome b
-
succinate dehydrogenase contains one heme b
-
cytochrome b-560

-
-
-
FAD

-
1 mol of covalently bound flavin per 100,000 g of protein; covalently bound to flavoprotein subunit
FAD
-
covalently bound to flavoprotein subunit
FAD
-
role in succinate oxidation
FAD
-
1 mol flavin per mol succinate dehydrogenase
FAD
-
covalently bound to flavoprotein subunit
FAD
-
covalently bound to flavoprotein subunit
FAD
-
covalently linked to protein histidyl residue
FAD
-
covalently bound to FRDA subunit
FAD
-
covalently linked to larger subunit
FAD
-
amino acid sequence around FAD-binding site
FAD
-
localized in Sdh1, i.e. the flavoprotein subunit
FAD
-
covalently attached to the enzyme to enable succinate oxidation
FAD
-
flavoprotein subunit SdhA
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
-
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
-
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
-
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
-
bound in the succinate dehydrogenase flavoprotein, SdhA, subunit
FAD
-
bound in the succinate dehydrogenase flavoprotein, SdhA, subunit
FAD
-
the enzyme complex contains one molecule of covalently bound FAD
FAD
-
SdhA is the FAD-containing 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
flavin

-
-
flavin
-
the enzyme complex contains non-extractable flavin. The purified complex contains 4.6 nmol/mg acid non-extractable flavin
flavin
-
quantitative determination of content in wild-type and mutant enzymes
flavin
flavoprotein of succinate dehydrogenase
flavin
-
covalently-bound flavin cofactor
flavin adenine dinucleotide

-
-
flavin adenine dinucleotide
-
-
heme

-
-
heme
-
single heme localized between Sdh3 and Sdh4 subunits
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
-
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
-
the enzyme contains two heme b cofactors, a di-heme
heme b

-
heme bP und heme bD
heme b
-
the enzyme contains one hydrophobic subunit (C) with two haem b groups
heme b
-
the quinone binding site of succinate dehydrogenase is required for electron transfer to the heme b
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
-
SdhB
phenazine methosulfate

-
-
phenazine methosulfate
-
-
ubiquinone

-
-
ubiquinone
-
two putative binding sites in the di-heme membrane anchoring protein
ubiquinone
-
the residues required for quinone-binding are harbored by SdhD
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 enzyme contains iron-sulfur centers; 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
-
measurement of the redox potentials of the sulfur-centers; the enzyme contains iron-sulfur centers
-
additional information
-
measurement of the redox potentials of the sulfur-centers; 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 18-20% lipid by weight protein
-
additional information
-
the enzyme contains acid-labile sulfides
-
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; the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers; 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 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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.