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Information on EC 1.8.7.3 - ferredoxin:CoB-CoM heterodisulfide reductase for references in articles please use BRENDA:EC1.8.7.3
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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
2
oxidized ferredoxin [iron-sulfur] cluster
+
+
=
2
reduced ferredoxin [iron-sulfur] cluster
+
+
2
Synonyms
CoB-S-S-CoM reductase, Coenzyme B-Coenzyme M heterodisulfide reductase, hdrA1B1C1, hdrA2B2C2, HdrABC, HdrB, HdrB2, HdrB2C2, heterodisulfide reductase,
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CoB-S-S-CoM reductase
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Coenzyme B-Coenzyme M heterodisulfide reductase
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hdrA1B1C1
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gene name
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hdrA2B2C2
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gene name
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heterodisulfide reductase
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-
HdrABC
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gene name
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HdrB
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subunit
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2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM = 2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
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-
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CoB,CoM:ferredoxin oxidoreductase
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oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized methyl viologen + CoB + CoM
reduced methyl viologen + CoM-S-S-CoB + H+
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
r
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
?
oxidized methyl viologen + CoB + CoM
reduced methyl viologen + CoM-S-S-CoB + H+
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-
-
-
?
oxidized methyl viologen + CoB + CoM
reduced methyl viologen + CoM-S-S-CoB + H+
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-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
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-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
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-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
-
-
-
r
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
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-
-
-
?
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oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
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-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
r
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
-
-
-
-
?
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
Q50755
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?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
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-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
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-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + H+
oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
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-
-
r
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + DsrC-S-S-DsrC + H+
oxidized ferredoxin [iron-sulfur] cluster + DsrC + DsrC
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-
-
-
?
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[4Fe-4S]-center
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Zn2+
-
required
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0.05
CoM-S-S-CoB
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subunit HdrB2C2, at 21°C, pH not specified in the publication
1.1
CoB
-
subunit HdrB2, at 21°C, pH not specified in the publication
1.2
CoB
-
subunit HdrB2C2, at 21°C, pH not specified in the publication
1.2
CoM
-
subunit HdrB2, at 21°C, pH not specified in the publication
1.4
CoM
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subunit HdrB2C2, at 21°C, pH not specified in the publication
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brenda
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brenda
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brenda
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brenda
subunit HdrB
UniProt
brenda
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brenda
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brenda
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brenda
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HDRA1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
801
0
86966
Swiss-Prot
HDRA2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
793
0
86918
Swiss-Prot
HDRA_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
793
0
86803
Swiss-Prot
HDRB1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
314
0
35327
Swiss-Prot
HDRB2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
300
0
32819
Swiss-Prot
HDRB_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
300
0
33068
Swiss-Prot
HDRC1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
247
0
27921
Swiss-Prot
HDRC2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
161
0
18150
Swiss-Prot
HDRC_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
161
0
18120
Swiss-Prot
HDRB_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
302
0
33458
Swiss-Prot
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?
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x * 18000, subunit HdrC2, SDS-PAGE; x * 33000, subunit HdrB2, SDS-PAGE
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phenyl-Sepharose column chromatography, and Superdex 200 gel filtration
Q-Sepharose column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3)-pCodonPlus-RIL cells
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enzyme expression is upregulated in tetrathionate-grown cells
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Ramos, A.R.; Grein, F.; Oliveira, G.P.; Venceslau, S.S.; Keller, K.L.; Wall, J.D.; Pereira, I.A.
The FlxABCD-HdrABC proteins correspond to a novel NADH dehydrogenase/heterodisulfide reductase widespread in anaerobic bacteria and involved in ethanol metabolism in Desulfovibrio vulgaris Hildenborough
Environ. Microbiol.
17
2288-2305
2015
Desulfovibrio vulgaris, Desulfovibrio vulgaris ATCC 29579
brenda
Kroeninger, L.; Berger, S.; Welte, C.; Deppenmeier, U.
Evidence for the involvement of two heterodisulfide reductases in the energy-conserving system of Methanomassiliicoccus luminyensis
FEBS J.
283
472-483
2016
Methanomassiliicoccus luminyensis, Methanomassiliicoccus luminyensis DSM 25720
brenda
Yan, Z.; Wang, M.; Ferry, J.G.
A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea
mBio
8
e02285-16
2017
Methanosarcina acetivorans
brenda
Hamann, N.; Mander, G.J.; Shokes, J.E.; Scott, R.A.; Bennati, M.; Hedderich, R.
A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from Methanothermobacter marburgensis
Biochemistry
46
12875-12885
2007
Methanothermobacter marburgensis (Q50755)
brenda
Mangold, S.; Valdes, J.; Holmes, D.S.; Dopson, M.
Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus
Front. Microbiol.
10
17
2011
Acidithiobacillus caldus
brenda
Fielding, A.J.; Parey, K.; Ermler, U.; Scheller, S.; Jaun, B.; Bennati, M.
Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate quinone reductase
J. Biol. Inorg. Chem.
18
905-915
2013
Methanothermobacter marburgensis
brenda
Buan, N.R.; Metcalf, W.W.
Methanogenesis by Methanosarcina acetivorans involves two structurally and functionally distinct classes of heterodisulfide reductase
Mol. Microbiol.
75
843-853
2010
Methanosarcina acetivorans
brenda
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1.8.7.3 ferredoxin:CoB-CoM heterodisulfide reductase
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