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Information on EC 1.8.98.1 - dihydromethanophenazine:CoB-CoM heterodisulfide reductase and Organism(s) Methanothermobacter marburgensis and UniProt Accession Q50756

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IUBMB 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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Methanothermobacter marburgensis
UNIPROT: Q50756
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The taxonomic range for the selected organisms is: Methanothermobacter marburgensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
heterodisulfide reductase, hdrabc, hdrc2, h2:heterodisulfide oxidoreductase, hdra2b2c2, hdrc1, soluble heterodisulfide reductase, hdrb1, hdrb2, co:com-s-s-cob oxidoreductase system, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HdrB
-
catalytic subunit of HDR
HdrC
-
catalytic subunit of HDR
heterodisulfide reductase
soluble heterodisulfide reductase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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reduction
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.
CAS REGISTRY NUMBER
COMMENTARY hide
116515-35-6
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128172-71-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
show the reaction diagram
-
-
-
-
?
CoM-S-S-CoB + ?
CoM-SH + CoB-SH + ?
show the reaction diagram
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
show the reaction diagram
-
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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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Iron-sulfur cluster
the cluster is fixed by cysteines of two cysteine-rich CCG domain sequence motifs (CX31-39CCX35-36CXXC) of subunit HdrB of the Methanothermobacter marburgensis HdrABC complex. An Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain is performed
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of HdrB subunit in Bacillus subtilis
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subunit HdrB is produced in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Madadi-Kahkesh, S.; Duin, E.C.; Heim, S.; Albracht, S.P.; Johnson, M.K.; Hedderich, R.
A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea
Eur. J. Biochem.
268
2566-2577
2001
Methanosarcina barkeri, Methanothermobacter marburgensis
Manually annotated by BRENDA team
Duin, E.C.; Madadi-Kahkesh, S.; Hedderich, R.; Clay, M.D.; Johnson, M.K.
Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction
FEBS Lett.
512
263-268
2002
Methanothermobacter marburgensis
Manually annotated by BRENDA team
Duin, E.C.; Bauer, C.; Jaun, B.; Hedderich, R.
Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme M-treated enzyme
FEBS Lett.
538
81-84
2003
Methanosarcina barkeri, Methanothermobacter marburgensis
Manually annotated by BRENDA team
Shokes, J.E.; Duin, E.C.; Bauer, C.; Jaun, B.; Hedderich, R.; Koch, J.; Scott, R.A.
Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase
FEBS Lett.
579
1741-1744
2005
Methanothermobacter marburgensis
Manually annotated by BRENDA team
Hedderich, R.; Hamann, N.; Bennati, M.
Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
Biol. Chem.
386
961-970
2005
Methanosarcina barkeri, Methanosarcina thermophila, Methanothermobacter marburgensis
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Methanothermobacter marburgensis (Q50755), Methanothermobacter marburgensis DSM 2133 (Q50755)
Manually annotated by BRENDA team