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IUBMB CommentsThe 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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fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
Q65GF3; A0A0C5C6P0 AND
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-
-
?
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
Q65GF3; A0A0C5C6P0 AND
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-
-
?
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas
in the anaerobic respiratory chain
-
-
r
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas ATCC 19364
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
-
-
-
r
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Megalodesulfovibrio gigas ATCC 19364
-
-
-
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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fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas
in the anaerobic respiratory chain
-
-
r
fumarate + menaquinol + 2 H+[side 2]
succinate + menaquinone + 2 H+[side 1]
Megalodesulfovibrio gigas ATCC 19364
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
-
-
-
r
succinate + menaquinone + 2 H+[side 1]
fumarate + menaquinol + 2 H+[side 2]
Megalodesulfovibrio gigas ATCC 19364
-
-
-
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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Q65GF3: cytochrome b558 subunit sdhC, A0A0C5C6P0: flavoprotein subunit sdhA, A0A0C5C686: reductase iron-sulfur protein sdhB
Q65GF3; A0A0C5C6P0 AND
UniProt
brenda
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brenda
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brenda
Megalodesulfovibrio gigas
T2G9X8: iron-sulfur subunit, T2GAT5: cytochrome b subunit, T2GB49: flavoprotein subunit
UniProt
brenda
Megalodesulfovibrio gigas ATCC 19364
T2G9X8: iron-sulfur subunit, T2GAT5: cytochrome b subunit, T2GB49: flavoprotein subunit
UniProt
brenda
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-
brenda
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brenda
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-
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
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-
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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homodimer
Megalodesulfovibrio gigas
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
-
x * 65000 + x * 28000 + x * 23000
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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oligomer
-
x * 65000 + x * 28000 + x * 23000
oligomer
-
x * 75000 + x * 28000 + x * 27000
oligomer
-
x * 70000 + x * 32000 + x * 18000
oligomer
-
x * 63000 + x * 27000 + x * 15000 + x * 14000
oligomer
-
x * 64000 + x * 27000 + x * 15000 + x * 14000
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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