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Information on EC 1.8.98.1 - dihydromethanophenazine:CoB-CoM heterodisulfide reductase
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1.8.98.1 dihydromethanophenazine:CoB-CoM heterodisulfide reductaseIUBMB Comments
This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase and EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase.
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Word Map
- 1.8.98.1
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methanogen
- hydrogenase
- methanosarcina
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methanogenesis
- acidithiobacillus
- barkeri
- methanothermobacter
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energy-conserving
-
flavin-based
-
hydrogenotrophic
- cob-sh
- marburgensis
-
aceticlastic
- 2-hydroxyphenazine
-
sulfur-oxidizing
- formylmethanofuran
- methanosarcinales
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endergonic
- methanomicrobiales
- dsrc
-
f420-reducing
- hs-cob
The enzyme appears in viruses and cellular organisms
Synonyms
heterodisulfide reductase, hdrabc, hdrc2, h2:heterodisulfide oxidoreductase, hdra2b2c2, hdrc1, soluble heterodisulfide reductase, hdrb1, hdrb2, co:com-s-s-cob oxidoreductase system, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CoM-S-S-HTP reductase
DsrK
-
homologue to the HdrD subunit of heterodisulfide reductase
F420H2-dependent CoM-S-S-HTP reductase
F420H2-dependent heterodisulfide reductase
ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase
-
-
H2:heterodisulfide oxidoreductase
HDR
HdrA
HdrABC
HdrB1
HdrB2
HdrC1
HdrC2
HdrD
heterodisulfide reductase
SdhC
soluble heterodisulfide reductase
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-
-
-
additional information
heterodisulfide reductase
-
-
-
-
additional information
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the H2:heterodisulfide oxidoreductase multienzyme complex is composed of nine polypeptides with MW 46000 Da, 39000 Da, 28000 Da, 25000 Da, 23000 Da, 21000 Da, 20000 Da, 16000 Da, 15000 Da
additional information
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H2:heterodisulfide oxidoreductase complex consists of F420-non-reducing hydrogenase and heterodisulfide reductase
additional information
-
H2:heterodisulfide oxidoreductase complex consists of F420-non-reducing hydrogenase and heterodisulfide reductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CoB + CoM + methanophenazine = CoM-S-S-CoB + dihydromethanophenazine
highly specific
-
-
-
CoB + CoM + methanophenazine = CoM-S-S-CoB + dihydromethanophenazine
This enzyme is found in methanogenic archaea, particularly Methanosarcina species, and regenerates coenzyme M and coenzyme B after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. Contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. Highly specific for both coenzyme M and coenzyme B. Reacts with various phenazine derivatives, including 2-hydroxyphenazine and 2-bromophenazine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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reduction
reduction
-
-
-
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reduction
-
the enzyme reduces the heterodisulfide CoM-S-S-CoB of the methanogenic thiol-coenzymes, coenzyme M and coenzyme B
reduction
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the enzyme reduces the heterodisulfide CoM-S-S-CoB of the methanogenic thiol-coenzymes, coenzyme M and coenzyme B
reduction
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the enzyme reduces the heterodisulfide CoM-S-S-CoB of the methanogenic thiol-coenzymes, coenzyme M and coenzyme B
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
CoB:CoM:methanophenazine oxidoreductase
This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase and EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase.
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CAS REGISTRY NUMBER
COMMENTARY
116515-35-6
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128172-71-4
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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 + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methylene blue
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
-
-
-
-
?
coenzyme B + coenzyme M + reduced ferredoxin + H+ + coenzyme F420
coenzyme B-coenzyme M disulfide + ferredoxin + H2 + reduced coenzyme F420
-
-
-
-
?
coenzyme B-coenzyme M disulfide + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
coenzyme B-coenzyme M disulfide + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
coenzyme B-coenzyme M disulfide + reduced methyl viologen
coenzyme B + coenzyme M + methyl viologen
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydro-2-hydroxyphenazine
coenzyme B + coenzyme M
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced 2-bromophenazine
coenzyme B + coenzyme M + 2-bromophenazine
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced 2-hydroxyphenazine
coenzyme B + coenzyme M + 2-hydroxyphenazine
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzylviologen
coenzyme B + coenzyme M + benzylviologen
-
-
-
-
?, r
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzylviologen
coenzyme B + coenzyme M + oxidized benzyl viologen
-
reaction intermediate is a [4Fe-4S]3+ cluster that is coordinated by one of the cysteines of nearby active-site disulfide or by the sulfur of coenzyme M
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-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced cytochrome b
coenzyme B + coenzyme M + oxidized cytochrome b
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methyl viologen
coenzyme B + coenzyme M + methyl viologen
-
ping-pong mechanism
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
coenzyme B + coenzyme M + methylene blue
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methyl viologen
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methylviologen
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + oxidized methylviologen
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced phenazine-1-carboxylic acid
coenzyme B + coenzyme M + phenazine-1-carboxylic acid
-
-
-
-
?
coenzyme B + 6-mercaptohexanoyl-L-threonine phosphate + methylene blue
? + methylene blue
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-
-
-
ir
coenzyme B + 6-mercaptohexanoyl-L-threonine phosphate + methylene blue
? + methylene blue
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-
-
-
ir
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B-coenzyme M disulfide + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
-
-
-
-
?
coenzyme B-coenzyme M disulfide + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced ferredoxin
coenzyme B + coenzyme M + ferredoxin
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced ferredoxin
coenzyme B + coenzyme M + ferredoxin
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced methyl viologen
coenzyme B + coenzyme M + methyl viologen
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced methyl viologen
coenzyme B + coenzyme M + methyl viologen
-
-
-
-
?
DsrC protein disulfide + dihydromethanophenazine
DsrC protein + methanophenazine
-
-
-
-
r
DsrC protein disulfide + dihydromethanophenazine
DsrC protein + methanophenazine
-
-
-
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r
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
-
reaction is coupled with the transfer of protons across the membrane of washed vesicles, which drives ATP formation from ADP
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
-
ping-pong mechanism
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
energy-conserving step in methanohenic archaea
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
reaction is coupled with transfer of protons across the cytoplasmic membrane. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP plus phosphate. Two different proton-translocating segments are present in the H2:heterodisulfide oxidoreductase system. The first involves the 2-hydroxyphenazine-dependent hydrogenase, and the second involves the heterodisulfide reductase
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
reaction is independent of coenzyme F420. Reaction is coupled to proton translocation across the cytoplasmic membrane into the lumen of the everted vesicle. The transmembrane electrochemical gradient thereby generated unduces ATP synthesis from ADP + phosphate
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
energy-conserving step
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
the D-enantiomer of the heterodisulfide is reduced at approximately 35% of the rate observed for the L-form
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
the D-enantiomer of the heterodisulfide is reduced at approximately 35% of the rate observed for the L-form
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
energy-conserving step
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
-
reaction intermediate is a [4Fe-4S]3+ cluster that is coordinated by one of the cysteines of nearby active-site disulfide or by the sulfur of coenzyme M
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced cytochrome b
coenzyme B + coenzyme M + oxidized cytochrome b
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced cytochrome b
coenzyme B + coenzyme M + oxidized cytochrome b
-
electron transfer by a CO dehydrogenase in complex with the heterodisulfide oxidoreductase, no H2 uptake in vivo, reaction is part of the overall reduction of acetate to methane and H2O, also providing a proton-translocation redox system to drive ATP formation
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
coenzyme B + coenzyme M + methylene blue
-
-
-
-
r
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
coenzyme B + coenzyme M + methylene blue
-
-
-
-
r
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methyl viologen
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methyl viologen
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methylviologen
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methylviologen
-
-
-
-
?
additional information
?
-
-
Hdr complexes with F420-nonreducing hydrogenase, formate dehydrogenase, and formyl-MFR dehydrogenase, model of complex of proteins that interact with Hdr, overview
-
-
?
additional information
?
-
-
Hdr complexes with F420-nonreducing hydrogenase, formate dehydrogenase, and formyl-MFR dehydrogenase, model of complex of proteins that interact with Hdr, overview
-
-
?
additional information
?
-
-
no activity with the homodisulfides of coenzyme M and coenzyme B
-
-
?
additional information
?
-
-
no activity with the homodisulfides of coenzyme M and coenzyme B
-
-
?
additional information
?
-
-
homodisulfides of coenzyme M and coenzyme B are not reduced
-
-
?
additional information
?
-
-
the enzyme does not catalyze the reduction of N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine with NADH, NADPH or reduced coenzyme F420
-
-
?
additional information
?
-
-
homodisulfides of coenzyme M and coenzyme B are not reduced
-
-
?
additional information
?
-
-
the enzyme does not catalyze the reduction of N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine with NADH, NADPH or reduced coenzyme F420
-
-
?
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NATURAL SUBSTRATE
NATURAL 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 + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
coenzyme B-coenzyme M disulfide + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced cytochrome b
coenzyme B + coenzyme M + oxidized cytochrome b
-
electron transfer by a CO dehydrogenase in complex with the heterodisulfide oxidoreductase, no H2 uptake in vivo, reaction is part of the overall reduction of acetate to methane and H2O, also providing a proton-translocation redox system to drive ATP formation
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B + coenzyme M + methanophenazine
N-[7-[(2-sulfoethyl)dithio]heptanoyl]-O3-phospho-L-threonine + dihydromethanophenazine
-
-
-
-
?
coenzyme B-coenzyme M disulfide + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
-
-
-
-
?
coenzyme B-coenzyme M disulfide + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced ferredoxin
coenzyme B + coenzyme M + ferredoxin
-
-
-
-
?
coenzyme B-coenzyme M disulfide + reduced ferredoxin
coenzyme B + coenzyme M + ferredoxin
-
-
-
-
?
DsrC protein disulfide + dihydromethanophenazine
DsrC protein + methanophenazine
-
-
-
-
r
DsrC protein disulfide + dihydromethanophenazine
DsrC protein + methanophenazine
-
-
-
-
r
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
-
reaction is coupled with the transfer of protons across the membrane of washed vesicles, which drives ATP formation from ADP
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
energy-conserving step in methanohenic archaea
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
reaction is coupled with transfer of protons across the cytoplasmic membrane. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP plus phosphate. Two different proton-translocating segments are present in the H2:heterodisulfide oxidoreductase system. The first involves the 2-hydroxyphenazine-dependent hydrogenase, and the second involves the heterodisulfide reductase
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
energy-conserving step
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
-
energy-conserving step
-
-
?
additional information
?
-
-
Hdr complexes with F420-nonreducing hydrogenase, formate dehydrogenase, and formyl-MFR dehydrogenase, model of complex of proteins that interact with Hdr, overview
-
-
?
additional information
?
-
-
Hdr complexes with F420-nonreducing hydrogenase, formate dehydrogenase, and formyl-MFR dehydrogenase, model of complex of proteins that interact with Hdr, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
subunit HdrB contains a Fe-S cluster fixed by cysteines of two cysteine-rich CCG domain sequence motifs, CX31-39CCX35-36CXXC. Electron paramagnetic resonance spectra are consistent with with the attachment of the substrate to the cluster in HdrABC and infer that the cluster's magnetic properties arise from the CCG binding motif
cytochrome b
-
the 23000 Da subunit is the cytochrome b, cytochrome b serves as electron donor for the heterodisulfide reduction
-
cytochrome b
-
the H2:heterodisulfide oxidoreductase multienzyme complex contains 3.2 nmol cytochrome b per mg protein
-
FAD
-
1 mol H2: heterodisulfide oxidoreductase complex with MW 250000 Da contains approximately 0.9 mol FAD
FAD
-
enzyme contains 4 mol FAD per mol of native enzyme
FAD
-
the H2:heterodisulfide oxidoreductase multienzyme complex contiams 0.6 nmol per mg of protein
heme
-
contains two b-hemes. Only the low spin heme and the high potential FeS cluster are involved in reduction of N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine
heme
-
the enzyme contains two discrete b-type hemes in the small subunit. One heme is high-spin and has a high midpoint potential, -23 mV, whereas the other heme is low-spin and exhibits a relatively low midpoint potential, -180 mV
additional information
-
no reaction with conenzyme F420
-
additional information
not a flavoenzyme, both subunits lack an FAD-binding motif
-
additional information
-
not a flavoenzyme, both subunits lack an FAD-binding motif
-
additional information
-
the H2:heterodisukfide oxidoreductase complex does not mediate the reduction of coenzyme F420 with H2 nor the oxidation of reduced coenzyme F420 with the heterodisulfide
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
-
the purified catalytic subunit HrdD contains 7.0 mol non-heme iron per mol monomer
Fe2+
-
[2Fe-2S] cluster core with complete cysteinyl ligation in center C, sensitive to dithionite
Iron
Ni
Zn2+
Iron
-
coenzyme M binds to a [4Fe-4S] cluster in the active site
Iron
-
the enzyme contains 280 nmol of non-heme iron per mg of protein
Iron
-
the H2:heterodisulfide oxidoreductase multienzyme complex contains 70-80 nmol non-heme iron and acid labile sulfur per mg of protein
Iron
-
contains two [Fe4S4] clusters. Only the low spin heme and the high potential FeS cluster are involved in reduction of N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine. A 4 Fe cluster is the initial electron acceptor
Iron
-
the enzyme contains two distinct [Fe4S4]2+/1+ clusters in the large subunit
Iron
-
active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction