1.8.98.5: H2:CoB-CoM heterodisulfide,ferredoxin reductase
This is an abbreviated version!
For detailed information about H2:CoB-CoM heterodisulfide,ferredoxin reductase, go to the full flat file.
Word Map on EC 1.8.98.5
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1.8.98.5
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methanococcus
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methanogenic
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hydrogenases
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archaea
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nickel
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epr
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voltae
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sulfur
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methanosarcina
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energy-conserving
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ni
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hyperfine
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methanobacterium
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selenocysteine
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f420-reducing
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fad
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heterolytic
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methane
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selenium-containing
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barkeri
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illumination
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selenium
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thermoautotrophicum
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com-s-s-cob
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methanothermobacter
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hydrogenotrophic
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non-heme
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marburgensis
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acid-labile
- 1.8.98.5
- methanococcus
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methanogenic
- hydrogenases
- archaea
- nickel
- epr
- voltae
- sulfur
- methanosarcina
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energy-conserving
- ni
-
hyperfine
-
methanobacterium
- selenocysteine
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f420-reducing
- fad
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heterolytic
- methane
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selenium-containing
- barkeri
- illumination
- selenium
- thermoautotrophicum
- com-s-s-cob
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methanothermobacter
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hydrogenotrophic
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non-heme
- marburgensis
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acid-labile
Reaction
2 reduced ferredoxin [iron-sulfur] cluster + + + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster +
Synonyms
CoB-CoM heterodisulfide reductase, F420-non-reducing hydrogenase, H2-driven FBEB, H2: CoM-S-S-CoB oxidoreductase, H2: heterodisulfide oxidoreductase complex, HdrA, hdrA1B1C1, HdrABC, HdrABC-MvhAGD, HdrB, HdrC, HdrDE, HdrDE-VhoGAC, heterodisulfide reductase, heterodisulfide reductase complex, hydrogenase, More, Mvh, MvhA, MvhADG, MvhADG/HdrABC, MvhD, MvhG, VhoGAC, Vhu
ECTree
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Substrates Products
Substrates Products on EC 1.8.98.5 - H2:CoB-CoM heterodisulfide,ferredoxin reductase
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REACTION DIAGRAM
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Vdu containing complexes show higher activity with hydrogen compared to formate. H2 oxidation by FBEB by the MvhHdr complex reduces ferredoxin (Fd) to almost 100%
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Vdu containing complexes show higher activity with hydrogen compared to formate. H2 oxidation by FBEB by the MvhHdr complex reduces ferredoxin (Fd) to almost 100%
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
Methanosarcina barkeri MS DSM 800
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
HdrABC catalyzes the CoM-S-S-CoB-dependent reduction of ferredoxin with H2, coupling the endergonic reduction of ferredoxin to the exergonic reduction of coenzyme B-coenzyme M disulfide. Per mole CoM-S-S-CoB added, 1 mol of ferredoxin is reduced, indicating an electron bifurcation coupling mechanism. The stoichiometry of coupling is consistent with an ATP gain per mole methane from 4 H2 and CO2 of near 0.5
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coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
HdrABC catalyzes the CoM-S-S-CoB-dependent reduction of ferredoxin with H2, coupling the endergonic reduction of ferredoxin to the exergonic reduction of coenzyme B-coenzyme M disulfide. Per mole CoM-S-S-CoB added, 1 mol of ferredoxin is reduced, indicating an electron bifurcation coupling mechanism. The stoichiometry of coupling is consistent with an ATP gain per mole methane from 4 H2 and CO2 of near 0.5
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coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
purified complex shows a twofold higher specific activity with ferredoxin than with metronidazole
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coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
purified complex shows a twofold higher specific activity with ferredoxin than with metronidazole
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reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus
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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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reduced methyl viologen + CoB + CoM + H+
Methanobacterium thermoautotrophicus
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H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
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H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
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H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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H2 + oxidized metronidazole + CoM-S-S-CoB
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reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
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Methanobacterium thermoautotrophicus
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no activity with coenzyme F420
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additional information
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Methanobacterium thermoautotrophicus DSM 2133
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no activity with coenzyme F420
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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the non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
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additional information
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the non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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