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EC Tree
IUBMB Comments This enzyme complex is found in H2-oxidizing CO2-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus. It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase. Electron pairs donated by the hydrogenase are transferred via its delta subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
reduced ferredoxin [iron-sulfur] cluster
+
+
+
2
=
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
Synonyms
f420-non-reducing hydrogenase, mvhadg, mvhadg/hdrabc,
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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
-
-
HdrA
-
HdrABC
-
HdrB
-
HdrC
-
Mvh
-
-
MvhA
-
subunit
MvhADG
-
MvhADG/HdrABC
-
-
MvhD
-
subunit
MvhG
-
subunit
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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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CoB,CoM,ferredoxin:H2 oxidoreductase
This enzyme complex is found in H2-oxidizing CO2-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus. It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase. Electron pairs donated by the hydrogenase are transferred via its delta subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
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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
?
-
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
-
?
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
-
?
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
-
?
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
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 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+
Methanobacterium thermoautotrophicus
-
-
-
?
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
?
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + 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 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
-
-
-
?
reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
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-
-
?
additional information
?
-
Methanobacterium thermoautotrophicus
-
no activity with coenzyme F420
-
?
additional information
?
-
Methanobacterium thermoautotrophicus DSM 2133
-
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
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 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
-
-
-
-
?
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
-
the enzyme contains approximately 0.9 mol nickel
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Fe2+
Methanobacterium thermoautotrophicus
-
the enzyme contains approximately 26 mol non-heme iron
Ni2+
Methanobacterium thermoautotrophicus
-
the enzyme contains approximately 0.6 mol nickel
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coenzyme F430
Methanobacterium thermoautotrophicus
-
-
potassium phosphate
Methanobacterium thermoautotrophicus
-
-
potassium phosphate
complex is most active in presence of 1.6 M potassium phosphate
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110
HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60°C
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7.5
-
-
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70
-
-
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Methanobacterium thermoautotrophicus
-
-
-
brenda
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
brenda
-
-
-
brenda
subunit HrdA
UniProt
brenda
subunit HrdB
UniProt
brenda
subunit HrdC
UniProt
brenda
-
-
-
brenda
subunit HrdA
UniProt
brenda
subunit HrdB
UniProt
brenda
subunit HrdC
UniProt
brenda
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-
brenda
-
-
brenda
Methanobacterium thermoautotrophicus
-
-
-
brenda
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
brenda
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HDRB2_METMP
Methanococcus maripaludis (strain S2 / LL)
293
0
32026
Swiss-Prot
-
HDRB_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
302
0
33513
Swiss-Prot
-
HDRB_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
302
0
33458
Swiss-Prot
-
HDRC1_METMP
Methanococcus maripaludis (strain S2 / LL)
192
0
21600
Swiss-Prot
-
HDRC2_METMP
Methanococcus maripaludis (strain S2 / LL)
184
0
20452
Swiss-Prot
-
HDRC_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
185
0
20490
Swiss-Prot
-
HDRC_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
185
0
20520
Swiss-Prot
-
HDRA_METMP
Methanococcus maripaludis (strain S2 / LL)
658
0
71281
Swiss-Prot
-
HDRA_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
659
0
72392
Swiss-Prot
-
HDRA_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
659
0
72182
Swiss-Prot
-
HDRB1_METMP
Methanococcus maripaludis (strain S2 / LL)
301
0
33510
Swiss-Prot
-
A0A485LW64_9ZZZZ
520
0
56536
TrEMBL
other Location (Reliability: 2 )
A0A482UYU8_9EURY
141
0
15989
TrEMBL
-
A0A482V6D5_9EURY
755
0
82703
TrEMBL
-
A0A485LV16_9ZZZZ
76
0
7955
TrEMBL
other Location (Reliability: 1 )
A0A482V602_9EURY
441
0
49666
TrEMBL
-
A0A485LWP9_9ZZZZ
200
0
22565
TrEMBL
other Location (Reliability: 2 )
A0A482V4U2_9EURY
198
0
22644
TrEMBL
-
A0A485LVC7_9ZZZZ
310
0
33418
TrEMBL
other Location (Reliability: 2 )
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250000
Methanobacterium thermoautotrophicus
-
gel filtration
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?
-
x * 51000 + x * 41000 + x * 17000, SDS-PAGE
?
-
x * 51000 + x * 41000 + x * 17000, SDS-PAGE
heterohexamer
Methanobacterium thermoautotrophicus
-
2 * 80000 + 2 * 51000 + 2 * 41000 + 2 * 36000 + 2 * 21000 + 2 * 17000, SDS-PAGE
heterohexamer
Methanobacterium thermoautotrophicus DSM 2133
-
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
-
DEAE-Sepharose column chromatography, phenyl-Sepharose column chromatography, and hydroxyapatite column chromatography
Methanobacterium thermoautotrophicus
-
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
-
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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 (Q50754), Methanothermobacter marburgensis (Q50755), Methanothermobacter marburgensis (Q50756), Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133 (Q50754), Methanothermobacter marburgensis DSM 2133 (Q50755), Methanothermobacter marburgensis DSM 2133 (Q50756)
brenda
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
brenda
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
brenda
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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1.8.98.5 H2:CoB-CoM heterodisulfide,ferredoxin reductase
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