Information on EC 1.3.5.1 - succinate dehydrogenase

for references in articles please use BRENDA:EC1.3.5.1
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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.5.1
-
RECOMMENDED NAME
GeneOntology No.
succinate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinate + a quinone = fumarate + a quinol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aerobic respiration I (cytochrome c)
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aerobic respiration II (cytochrome c) (yeast)
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aerobic respiration III (alternative oxidase pathway)
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methylaspartate cycle
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succinate to cytochrome bd oxidase electron transfer
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succinate to cytochrome bo oxidase electron transfer
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superpathway of glyoxylate cycle and fatty acid degradation
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TCA cycle I (prokaryotic)
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TCA cycle II (plants and fungi)
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TCA cycle III (animals)
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TCA cycle IV (2-oxoglutarate decarboxylase)
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TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
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TCA cycle VII (acetate-producers)
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citric acid cycle
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propionate fermentation
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Citrate cycle (TCA cycle)
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Oxidative phosphorylation
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Butanoate metabolism
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Carbon fixation pathways in prokaryotes
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
succinate:quinone oxidoreductase
A flavoprotein (FAD) complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria and archaea. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. cf. EC 1.3.5.4, fumarate reductase (quinone).
CAS REGISTRY NUMBER
COMMENTARY hide
9002-02-2
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9028-11-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strains MRK,Webster, NY8, USG3 and Bridgeport grown in HL-60 cells, genes sdhA, sdhB, sdhC and sdhD
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
harbors the entire sdh operon on a low copy number plasmid
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
succinate dehydrogenase
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
facultative anaerobic bacterium
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Manually annotated by BRENDA team
soybean, succinate dehydrogenase
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Manually annotated by BRENDA team
single copy sdhB gene, encoding the iron-sulfur protein (Ip) subunit of succinate dehydrogenase, Sdh
UniProt
Manually annotated by BRENDA team
single copy sdhB gene, encoding the iron-sulfur protein (Ip) subunit of succinate dehydrogenase, Sdh
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
succinate dehydrogenase
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
fumarate reductase
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
B1YBY7: flavoprotein subunit, B1YBY8: ferredoxin
B1YBY7 and B1YBY8
UniProt
Manually annotated by BRENDA team
B1YBY7: flavoprotein subunit, B1YBY8: ferredoxin
B1YBY7 and B1YBY8
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
fumarate reductase
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Manually annotated by BRENDA team
gene sdh2s
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Manually annotated by BRENDA team
Chinese strain
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Manually annotated by BRENDA team
Chinese strain
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Manually annotated by BRENDA team
NCIMB400
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Manually annotated by BRENDA team
MR-1
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Manually annotated by BRENDA team
Shewanella oneidensis MR-1 / ATCC 700550
MR-1
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Manually annotated by BRENDA team
gene SDH2-2, encoding the iron sulfur subunit of the succinate dehydrogenase protein complex
UniProt
Manually annotated by BRENDA team
two SDG isoforms with different electrophoretic mobility
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Manually annotated by BRENDA team
two SDG isoforms with different electrophoretic mobility
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Manually annotated by BRENDA team
Staphylococcus aureus in biofilms, genes sdhCAB
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Manually annotated by BRENDA team
Staphylococcus aureus in biofilms, genes sdhCAB
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Manually annotated by BRENDA team
Staphylococcus aureus in biofilms, genes sdhCAB
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Manually annotated by BRENDA team
P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, P77946: subunit sdhD
P77943 and P77944 and P77945 and P77946
UniProt
Manually annotated by BRENDA team
P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, P77946: subunit sdhD
P77943 and P77944 and P77945 and P77946
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Manually annotated by BRENDA team
mung bean, succinate dehydrogenase
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Manually annotated by BRENDA team
gene sdh1-2
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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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 quinol–fumarate 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
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
show the reaction diagram
-
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
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?
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
fumarate + menaquinol
succinate + menaquinone
show the reaction diagram
-
fumarate reductase acts as part of an anaerobic respiratory chain
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r
fumarate + quinol
succinate + ubiquinone
show the reaction diagram
fumarate + reduced acceptor
succinate + acceptor
show the reaction diagram
fumarate + reduced benzyl viologen
succinate + benzyl viologen
show the reaction diagram
fumarate + reduced benzyl viologen
succinate + oxidized benzyl viologen
show the reaction diagram
-
-
-
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r
fumarate + reduced decylubiquinone
succinate + decylubiquinone
show the reaction diagram
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-
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r
fumarate + reduced phenazine methosulfate
succinate + phenazine methosulfate
show the reaction diagram
-
enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities
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r
fumarate + reduced plumbagin
succinate + oxidized plumbagin
show the reaction diagram
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?
succinate + 1,4-naphthoquinone
fumarate + 1,4-naphthoquinol
show the reaction diagram
succinate + 1-methoxy-5-methylphenazinium methyl sulfate
fumarate + ?
show the reaction diagram
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-
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?
succinate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinol
show the reaction diagram
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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
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?
succinate + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-1,4-benzohydroquinone
show the reaction diagram
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-
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?
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
show the reaction diagram
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?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
show the reaction diagram
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
show the reaction diagram
succinate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol
show the reaction diagram
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r
succinate + 2,3-dimethyl-1,4-naphthoquinone
fumarate + 2,3-dimethyl-1,4-naphthoquinol
show the reaction diagram
-
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
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r
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
succinate + 2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
?
show the reaction diagram
-
i.e. MTT, in presence of phenazine methosulfate, i.e. PMS
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?
succinate + 2-ethyl-3-methyl-1,4-naphthoquinone
fumarate + 2-ethyl-3-methyl-1,4-naphthoquinol
show the reaction diagram
-
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
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?
succinate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone
fumarate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol
show the reaction diagram
-
the succinate dehydrogenase C subunit is responsible for ubiquinone binding
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?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
succinate + benzyl viologen
fumarate + reduced benzyl viologen
show the reaction diagram
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?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
succinate + decylubiquinone
fumarate + ?
show the reaction diagram
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-
-
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?
succinate + decylubiquinone
fumarate + decylubiquinol
show the reaction diagram
succinate + decylubiquinone
fumarate + reduced decylubiquinone
show the reaction diagram
-
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r
succinate + duroquinone
fumarate + duroquinol
show the reaction diagram
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
succinate + FAD
fumarate + FADH2
show the reaction diagram
succinate + ferricyanide
fumarate + ferrocyanide
show the reaction diagram
-
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
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?
succinate + ferrocyanide
fumarate + ferricyanide
show the reaction diagram
succinate + menadione
fumarate + menadiol
show the reaction diagram
-
with 2,6-dichlorophenolindophenol
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?
succinate + menaquinone
fumarate + menaquinol
show the reaction diagram
succinate + nitro blue tetrazolium
fumarate + formazan
show the reaction diagram
-
yellow dye
blue dye
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?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
show the reaction diagram
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
succinate + oxidized benzyl viologen
fumarate + reduced benzyl viologen
show the reaction diagram
-
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r
succinate + oxidized donor
?
show the reaction diagram
-
endogenous SDH activity results in blue diphormazan deposits from the nitroblue tetrazolium reduction through succinate oxidation
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?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
show the reaction diagram
succinate + oxidized phenazine methosulfate
fumarate + reduced phenazine methosulfate
show the reaction diagram
-
-
-
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?
succinate + phenazine ethosulfate
fumarate + reduced phenazine ethosulfate
show the reaction diagram
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?
succinate + phenazine methosulfate
fumarate + ?
show the reaction diagram
-
phenazine methosulfate as direct electron acceptor and 2,6-dichlorophenolindophenol as final acceptor
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?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
show the reaction diagram
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
succinate + ubiquinone-1
fumarate + ubiquinol
show the reaction diagram
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
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r
succinate + ubiquinone-1
fumarate + ubiquinol-1
show the reaction diagram
succinate + ubiquinone-2
fumarate + ubiquinol
show the reaction diagram
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
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r
succinate + ubiquinone-8
fumarate + ubiquinol-8
show the reaction diagram
-
-
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r
succinate + WST-1
fumarate + reduced WST-1
show the reaction diagram
-
-
-
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?
ubiquinone-1 + L-malate
?
show the reaction diagram
ubiquinone-1 + succinate
ubiquinol + fumarate
show the reaction diagram
ubiquinone-1 + succinate
ubiquinol-1 + fumarate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
fumarate + menaquinol
succinate + menaquinone
show the reaction diagram
-
fumarate reductase acts as part of an anaerobic respiratory chain
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r
fumarate + reduced acceptor
succinate + acceptor
show the reaction diagram
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
active in aerobic respiration, repressed during anaerobic respiration
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?
succinate + FAD
fumarate + FADH2
show the reaction diagram
succinate + menaquinone
fumarate + menaquinol
show the reaction diagram
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methoxy-5-methylphenazinium methyl sulfate
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2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
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2,6-dichlorophenolindophenol
ATP
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activation
benzyl viologen
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cytochrome b
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cytochrome b-560
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cytochrome b558
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SdhC
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cytochrome c
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decylubiquinone
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Fe-S center
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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
flavin adenine dinucleotide
fumarate
-
activation
heme b
heme b556
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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
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the enzyme has a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
IDP
-
activation
iron-sulfur centre
phenazine methosulfate
Plumbagin
-
a quinone analogue
quinone
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with a periplasmically oriented quinone binding site of the enzyme
ubiquinone
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3Fe-4S center
4Fe-4S cluster
Q97W79 and Q97W78 and Q97W77 and Q97W76
the CCG-domain-containing subunit SdhE (formerly SdhC) contains a [4Fe–4S] cluster in reduced (2+) and oxidized (3+) states. The reduced form of the [4Fe–4S]2+ cluster is diamagnetic. The individual iron sites of the reduced cluster are noticeably heterogeneous and show partial valence localization, which is particularly strong for one unique ferrous site
Anions
Cl-
-
activates
ClO4-
-
activation
Fe-S cluster
Fe-S-clusters
fumarate
-
activation
I-
-
activation
iron-sulfur centre
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
K-edge X-ray absorption spectroscopy is used to monitor the structural changes of their Fe sites in the irreversible [2Fe-2S] cluster degradation process. Regardless of the differences in the cluster-ligating cysteine motifs and the XAS-detectable [2Fe-2S]2+ cluster environments, a complete reductive breakdown of the [2Fe-2S] clusters results in the appearance of a new Fourier transform peak at about 3.3 A with a concomitant loss of the Fe-Fe interaction at ca. 2.7 A for both proteins. The results suggest that a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de novo biosynthesis and/or regulation of iron-binding enzymes in the cellular system
Iron-sulfur cluster
K+
-
activates
malonate
-
activation
NO3-
-
activation
phosphate
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activation
SO42-
-
activation
succinate
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activation
[2Fe-2S]-center
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
the [2Fe-2S] cluster in SdhB-N and center C in SdhC are two succinate reducible high-potential centers detected in the archaeal succinate:caldariellaquinone oxidoreductase complex that differ in their arrangements of the cluster-binding cysteine motifs and the local cluster surroundings. a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de noVo biosynthesis and/or regulation of iron-binding enzymes in the cellular system