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Information on EC 1.8.98.5 - H2:CoB-CoM heterodisulfide,ferredoxin reductase
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The expected taxonomic range for this enzyme is: Methanothermobacter marburgensis
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EC NUMBER 
COMMENTARY 
1.8.98.5
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RECOMMENDED NAME
GeneOntology No.
H2:CoB-CoM heterodisulfide,ferredoxin reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
CoB,CoM,ferredoxin:H2 oxidoreductase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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+
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 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 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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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
potassium phosphate
complex is most active in presence of 1.6 M potassium phosphate; complex is most active in presence of 1.6 M potassium phosphate; complex is most active in presence of 1.6 M potassium phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110
HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60°C; HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60°C; HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.98.5)
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