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Information on EC 7.1.1.12 - succinate dehydrogenase (electrogenic, proton-motive force generating)
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7.1.1.12 succinate dehydrogenase (electrogenic, proton-motive force generating)IUBMB Comments
The enzyme is very similar to EC 1.3.5.1, succinate dehydrogenase, but differs by containing two heme molecules (located in the membrane anchor component) in addition to FAD and three iron-sulfur clusters. Unlike EC 1.3.5.1, this enzyme catalyses an electrogenic reaction, enabled by electron-bifurcation via the heme molecules. In the direction of succinate oxidation by menaquinone, which is endergonic, the reaction is driven by the transmembrane electrochemical proton potential. In the direction of fumarate reduction, the electrogenic electron transfer reaction is compensated by transmembrane proton transfer pathway known as the E-pathway, which results in overall electroneutrality.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
succinate:quinone oxidoreductases, quinol fumarate reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
quinol: fumarate reductase
SQR
succinate:quinone oxidoreductases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
succinate + menaquinone + 2 H+[side 1] = fumarate + menaquinol + 2 H+[side 2]
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
succinate:quinone oxidoreductase (electrogenic, proton-motive force generating)
The enzyme is very similar to EC 1.3.5.1, succinate dehydrogenase, but differs by containing two heme molecules (located in the membrane anchor component) in addition to FAD and three iron-sulfur clusters. Unlike EC 1.3.5.1, this enzyme catalyses an electrogenic reaction, enabled by electron-bifurcation via the heme molecules. In the direction of succinate oxidation by menaquinone, which is endergonic, the reaction is driven by the transmembrane electrochemical proton potential. In the direction of fumarate reduction, the electrogenic electron transfer reaction is compensated by transmembrane proton transfer pathway known as the E-pathway, which results in overall electroneutrality.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
Q65GF3; A0A0C5C6P0 AND
-
-
-
?
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
Q65GF3; A0A0C5C6P0 AND
-
-
-
?
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
in the anaerobic respiratory chain
-
-
r
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas ATCC 19364
T2G9X8; T2GAT5; T2GB49
in the anaerobic respiratory chain
-
-
r
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
in the direction of fumarate reduction, the electrogenic electron transfer reaction is compensated by transmembrane proton transfer pathway known as the E-pathway
-
-
?
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
in the direction of fumarate reduction, the electrogenic electron transfer reaction is compensated by transmembrane proton transfer pathway known as the E-pathway
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Q65GF3; A0A0C5C6P0 AND
the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Q65GF3; A0A0C5C6P0 AND
the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
-
-
-
r
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Megalodesulfovibrio gigas ATCC 19364
T2G9X8; T2GAT5; T2GB49
-
-
-
r
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
in the anaerobic respiratory chain
-
-
r
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas ATCC 19364
T2G9X8; T2GAT5; T2GB49
in the anaerobic respiratory chain
-
-
r
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
in the direction of fumarate reduction, the electrogenic electron transfer reaction is compensated by transmembrane proton transfer pathway known as the E-pathway
-
-
?
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
in the direction of fumarate reduction, the electrogenic electron transfer reaction is compensated by transmembrane proton transfer pathway known as the E-pathway
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Q65GF3; A0A0C5C6P0 AND
the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Q65GF3; A0A0C5C6P0 AND
the diheme-containing enzyme exploits the transmembrane electrochemical proton potential DELTAp to support the otherwise thermodynamically unfavorable oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
-
-
-
r
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Megalodesulfovibrio gigas ATCC 19364
T2G9X8; T2GAT5; T2GB49
-
-
-
r
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
the enzyme supports an electron transfer across the biological membranes in which it is embedded. The electrogenic reaction allows the transmembrane electrochemical proton potential DELTAp to drive the endergonic oxidation of succinate by menaquinone
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
-
-
?
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S cluster
the enzyme contains three iron-sulfur clusters
Fe-S cluster
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
the enzyme contains three iron-sulfur clusters
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe-S cluster
Fe-S cluster
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
the enzyme contains three iron-sulfur clusters
Fe-S cluster
the enzyme contains three iron-sulfur clusters
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-hydroxy-3-neopentyl-1,4-naphthoquinone
Q65GF3; A0A0C5C6P0 AND
competitive
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
2-hydroxy-3-neopentyl-1,4-naphthoquinone
Bacillus licheniformis
Q65GF3; A0A0C5C6P0 AND
pH and temperature not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
Q65GF3; A0A0C5C6P0 AND
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q65GF3: cytochrome b558 subunit sdhC, A0A0C5C6P0: flavoprotein subunit sdhA, A0A0C5C686: reductase iron-sulfur protein sdhB
Q65GF3; A0A0C5C6P0 AND
UniProt
brenda
Megalodesulfovibrio gigas
T2G9X8: iron-sulfur subunit, T2GAT5: cytochrome b subunit, T2GB49: flavoprotein subunit
T2G9X8; T2GAT5; T2GB49
UniProt
brenda
Megalodesulfovibrio gigas ATCC 19364
T2G9X8: iron-sulfur subunit, T2GAT5: cytochrome b subunit, T2GB49: flavoprotein subunit
T2G9X8; T2GAT5; T2GB49
UniProt
brenda
P17413: cytochrome b subunit, P17412: flavoprotein subunit, P17596: iron-sulfur subunit
SwissProt
brenda
P17413: cytochrome b subunit, P17412: flavoprotein subunit, P17596: iron-sulfur subunit
SwissProt
brenda
Q65GF3: cytochrome b558 subunit sdhC, A0A0C5C6P0: flavoprotein subunit sdhA, A0A0C5C686: reductase iron-sulfur protein sdhB
Q65GF3; A0A0C5C6P0 AND
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
oligomer
homodimer
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C
homodimer
Megalodesulfovibrio gigas ATCC 19364
-
each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C
-
oligomer
Q65GF3; A0A0C5C6P0 AND
1 * 23000 (cytochrome b558 subunit sdhC) + 1 * 65000 (flavoprotein subunit sdhA) + 1 * 28000 (reductase iron-sulfur protein sdhB), SDS-PAGE, homotrimeric complex of the heterotrimeric protomer
oligomer
-
1 * 23000 (cytochrome b558 subunit sdhC) + 1 * 65000 (flavoprotein subunit sdhA) + 1 * 28000 (reductase iron-sulfur protein sdhB), SDS-PAGE, homotrimeric complex of the heterotrimeric protomer
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method, crystal structure is determined at 3.6 A resolution
Megalodesulfovibrio gigas
T2G9X8; T2GAT5; T2GB49
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification, reconstitution into proteoliposomes, and functional characterization
Q65GF3; A0A0C5C6P0 AND
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guan, H.H.; Hsieh, Y.C.; Lin, P.J.; Huang, Y.C.; Yoshimura, M.; Chen, L.Y.; Chen, S.K.; Chuankhayan, P.; Lin, C.C.; Chen, N.C.; Nakagawa, A.; Chan, S.I.; Chen, C.J.
Structural insights into the electron/proton transfer pathways in the quinol fumarate reductase from Desulfovibrio gigas
Sci. Rep.
8
14935
2018
Megalodesulfovibrio gigas (T2G9X8 AND T2GAT5 AND T2GB49), Megalodesulfovibrio gigas ATCC 19364 (T2G9X8 AND T2GAT5 AND T2GB49)
brenda
Madej, M.; Nasiri, H.; Hilgendorff, N.; Schwalbe, H.; Unden, G.; Lancaster, C.
Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate menaquinone oxidoreductase from the Gram-positive bacterium Bacillus licheniformis
Biochemistry
45
15049-15055
2006
Bacillus licheniformis (Q65GF3 AND A0A0C5C6P0 AND), Bacillus licheniformis DSM 13 (Q65GF3 AND A0A0C5C6P0 AND)
brenda
Lancaster, C.
Wolinella succinogenes quinol fumarate reductase - 2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer
Biochim. Biophys. Acta
1565
215-231
2002
Wolinella succinogenes (P17413 AND P17412 AND P17596), Wolinella succinogenes, Wolinella succinogenes ATCC 29543 (P17413 AND P17412 AND P17596)
brenda
Lancaster, C.
The di-heme family of respiratory complex II enzymes
Biochim. Biophys. Acta
1827
679-687
2013
Bacillus subtilis, Bacillus licheniformis, Corynebacterium glutamicum, Thermus thermophilus, Rhodothermus marinus, Thermoplasma acidophilum
brenda
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Release 2023.1 (January 2023)
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