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Information on EC 1.8.98.5 - H2:CoB-CoM heterodisulfide,ferredoxin reductase for references in articles please use BRENDA:EC1.8.98.5Word Map on EC 1.8.98.5
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The expected taxonomic range for this enzyme is: Methanothermobacter marburgensis
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H2:CoB-CoM heterodisulfide,ferredoxin reductase
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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 regeneration IV (H2-dependent)
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Microbial metabolism in diverse environments
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CoB,CoM,ferredoxin:H2 oxidoreductase
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F420-non-reducing hydrogenase
H2: heterodisulfide oxidoreductase complex
F420-non-reducing hydrogenase
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F420-non-reducing hydrogenase
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H2: heterodisulfide oxidoreductase complex
Methanobacterium thermoautotrophicus
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H2: heterodisulfide oxidoreductase complex
Methanobacterium thermoautotrophicus DSM 2133
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HdrA
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HdrABC
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HdrB
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HdrC
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Mvh
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MvhA
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subunit
MvhADG
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MvhADG/HdrABC
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MvhD
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subunit
MvhG
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subunit
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Methanobacterium thermoautotrophicus
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Methanobacterium thermoautotrophicus DSM 2133
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subunit HrdA
UniProt
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subunit HrdB
UniProt
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subunit HrdC
UniProt
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subunit HrdA
UniProt
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subunit HrdB
UniProt
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subunit HrdC
UniProt
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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+
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
additional information
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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 + 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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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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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H2 + oxidized methyl viologen + CoM-S-S-CoB
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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reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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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reduced metronidazole + CoB + CoM + H+
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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additional information
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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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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
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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 ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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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FAD
Methanobacterium thermoautotrophicus
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the enzyme contains approximately 0.9 mol nickel
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Fe2+
Methanobacterium thermoautotrophicus
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the enzyme contains approximately 26 mol non-heme iron
Ni2+
Methanobacterium thermoautotrophicus
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the enzyme contains approximately 0.6 mol nickel
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coenzyme F430
Methanobacterium thermoautotrophicus
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potassium phosphate
Methanobacterium thermoautotrophicus
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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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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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7.5
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Methanobacterium thermoautotrophicus
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Methanobacterium thermoautotrophicus DSM 2133
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250000
Methanobacterium thermoautotrophicus
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gel filtration
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x * 51000 + x * 41000 + x * 17000, SDS-PAGE
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x * 51000 + x * 41000 + x * 17000, SDS-PAGE
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heterohexamer
Methanobacterium thermoautotrophicus
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2 * 80000 + 2 * 51000 + 2 * 41000 + 2 * 36000 + 2 * 21000 + 2 * 17000, SDS-PAGE
heterohexamer
Methanobacterium thermoautotrophicus DSM 2133
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2 * 80000 + 2 * 51000 + 2 * 41000 + 2 * 36000 + 2 * 21000 + 2 * 17000, SDS-PAGE
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DEAE-Sepharose and Q-Sepharose column chromatography, and Superdex 200 gel filtration
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DEAE-Sepharose column chromatography, phenyl-Sepharose column chromatography, and hydroxyapatite column chromatography
Methanobacterium thermoautotrophicus
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DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
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HDRA_METMP
Methanococcus maripaludis (strain S2 / LL)
658
71281
Swiss-Prot
HDRA_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
659
72392
Swiss-Prot
HDRA_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
659
72182
Swiss-Prot
HDRB1_METMP
Methanococcus maripaludis (strain S2 / LL)
301
33510
Swiss-Prot
HDRB2_METMP
Methanococcus maripaludis (strain S2 / LL)
293
32026
Swiss-Prot
HDRB_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
302
33513
Swiss-Prot
HDRB_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
302
33458
Swiss-Prot
HDRC1_METMP
Methanococcus maripaludis (strain S2 / LL)
192
21600
Swiss-Prot
HDRC2_METMP
Methanococcus maripaludis (strain S2 / LL)
184
20452
Swiss-Prot
HDRC_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
185
20490
Swiss-Prot
HDRC_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
185
20520
Swiss-Prot
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Kaster, A.; Moll, J.; Parey, K.; Thauer, R.
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
Proc. Natl. Acad. Sci. USA
108
2981-2986
2011
Methanothermobacter marburgensis, Methanothermobacter marburgensis (Q50754), Methanothermobacter marburgensis (Q50755), Methanothermobacter marburgensis (Q50756), Methanothermobacter marburgensis DSM 2133 (Q50754), Methanothermobacter marburgensis DSM 2133 (Q50755), Methanothermobacter marburgensis DSM 2133 (Q50756)
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Stojanowic, A.; Mander, G.; Duin, E.; Hedderich, R.
Physiological role of the F420-non-reducing hydrogenase (MvH) from Methanothermobacter marburgensis
Arch. Microbiol.
180
194-203
2003
Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133
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Setzke, E.; Hedderich, R.; Heiden, S.; Thauer, R.
H2 heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum Composition and properties
Eur. J. Biochem.
220
139-148
1994
Methanobacterium thermoautotrophicus, Methanobacterium thermoautotrophicus DSM 2133
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Kaster, A.; Moll, J.; Parey, K.; Thauer, R.
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
Proc. Natl. Acad. Sci. USA
108
2981-2986
2011
Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133
brenda
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