Information on EC 1.8.98.1 - CoB-CoM heterodisulfide reductase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.8.98.1
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RECOMMENDED NAME
GeneOntology No.
CoB-CoM heterodisulfide reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
coenzyme B + coenzyme M + methanophenazine = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine + dihydromethanophenazine
show the reaction diagram
highly specific; 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 hide
LITERATURE
oxidation
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reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme B/coenzyme M regeneration
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coenzyme M biosynthesis
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Methane metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
coenzyme B:coenzyme M:methanophenazine oxidoreductase
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 [3]. Highly specific for both coenzyme M and coenzyme B. Reacts with various phenazine derivatives, including 2-hydroxyphenazine and 2-bromophenazine.
CAS REGISTRY NUMBER
COMMENTARY hide
116515-35-6
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128172-71-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 27774
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Manually annotated by BRENDA team
strain 7
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Manually annotated by BRENDA team
strain 7
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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a cytoplasmic HdrABC enzyme complex is found in most methanogens, whereas a membrane-bound HdrED complex is found exclusively in members of the order Methanosarcinales. Multiple copies of both Hdr classes are found in all sequenced Methanosarcinales genomes. Evolutionary relationships among the Hdr proteins in methanogens, overview
metabolism
physiological function
additional information
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 + 6-mercaptohexanoyl-L-threonine phosphate + methylene blue
? + methylene blue
show the reaction diagram
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
show the reaction diagram
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
show the reaction diagram
coenzyme B + coenzyme M + methylene blue
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
show the reaction diagram
-
-
-
-
?
coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
show the reaction diagram
coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
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 + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydro-2-hydroxyphenazine
coenzyme B + coenzyme M
show the reaction diagram
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced 2-bromophenazine
coenzyme B + coenzyme M + 2-bromophenazine
show the reaction diagram
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-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced 2-hydroxyphenazine
coenzyme B + coenzyme M + 2-hydroxyphenazine
show the reaction diagram
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-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzyl viologen
coenzyme B + coenzyme M + benzyl viologen
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzylviologen
coenzyme B + coenzyme M + benzylviologen
show the reaction diagram
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-
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-
?, r
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzylviologen
coenzyme B + coenzyme M + oxidized benzyl viologen
show the reaction diagram
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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
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methyl viologen
coenzyme B + coenzyme M + methyl viologen
show the reaction diagram
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ping-pong mechanism
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-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue
coenzyme B + coenzyme M + methylene blue
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methyl viologen
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + methylviologen
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen
coenzyme B + coenzyme M + oxidized methylviologen
show the reaction diagram
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-
-
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?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced phenazine-1-carboxylic acid
coenzyme B + coenzyme M + phenazine-1-carboxylic acid
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
coenzyme B + coenzyme M + methanophenazine
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-O3-phospho-L-threonine + dihydromethanophenazine
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2
coenzyme B + coenzyme M + coenzyme F420
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine
coenzyme B + coenzyme M + methanophenazine
show the reaction diagram
-
-
-
-
?
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2
coenzyme B + coenzyme M
show the reaction diagram
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced cytochrome b
coenzyme B + coenzyme M + oxidized cytochrome b
show the reaction diagram
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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
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme F420
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cytochrome b
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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
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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[2Fe-2S] cluster core with complete cysteinyl ligation in center C, sensitive to dithionite
Zn2+
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enzyme contains an isolated zinc site
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R,3R)-3-hydroxy-2-([6-[(2-sulfoethyl)dithio]hexanoyl]amino)butanoic acid
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Ki above 2 mM
1,3-propanesulfone
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0.3 mM, 50% inhibition
Dithionite
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irreversible breakdown of the Fe-Fe interaction in the [2Fe-2S] cluster
iodoacetamide
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0.1 mM, 50% inhibition
NEM
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0.4 mM, 50% inhibition
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aquacobalamin
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stimulates the activity of the purified H2: heterodisulfide oxidoreductase complex
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
6-Mercaptohexanoyl-L-threonine phosphate
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pH 7.6, 54C
0.25
coenzyme B
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pH 7.0, 37C
0.2 - 0.8
coenzyme M
0.092
dihydromethanophenazine
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25C
0.03
H2
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pH 7, 65C, H2: heterodisulfide oxidoreductase complex
3
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-D-threonine
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pH 7.6, 65C
0.1 - 0.4
N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
74
dihydromethanophenazine
Methanosarcina thermophila
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25C
additional information
additional information
Methanothermobacter thermautotrophicus
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.6
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formation of the heterodisulfide, pH 7.6, 40C
0.62
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reduction of the heterodisulfide, pH 7.6, 40C
6
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reduction of the heterodisulfide with H2
24
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reduction of the heterodisulfide with benzylviologen
110
HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60C; HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60C; HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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H2:heterodisulfide oxidoreductase activity
7.6
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20C, Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
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activity with reduced benzyl viologen and N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine increases continously with decreasing pH in the range between pH 7.5 and pH 5.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
46000 Da subunit
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
155000
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gel filtration
206000
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equilibrium sedimentation
250000
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hexameric complex, H2:heterodisulfide oxidoreductase complex consisting of F420-non-reducing hydrogenase and heterodisulfide reductase, 20% is eluted as a dodecameric complex with MW 250000 Da, gel filtration
350000 - 400000
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gel filtration
550000
additional information
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MW of H2:heterodisulfide oxidoreductase multienzyme complex is 800000-1300000, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
comparison of molecular structure arrangement with enzymes from Escherichia coli, Methanococcus jannaschii or Wolinella succinogenes
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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30 min, 50% loss of activity
80
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rapid inactivation above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
more stable in presence of CHAPS than in the presence of dodecyl beta-D-maltoside
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
incubation of anaerobically prepared membranes in the presence of O2 results in a complete loss of activity within a few min
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654386
partially purified enzyme is insensitive towards O2
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639391
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, more than 80% inactivation within 12 h under aerobic conditions
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4C, under N2, partially purified enzyme, 50 mM Tris-HCl, pH 7.6, 0.5 M NaCl, loss of 20% activity within 24 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography, Q-Sepharose column chromatography and Superdex S200 column gel filtration
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H2:heterodisulfide oxidoreductase complex
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recombinant C-terminally His6-tagged HdrB1 and HdrB2 by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of HdrB1 and HdrB2 as C-terminally His6-tagged proteins in strain MM1263 and MM1264, respectively. The His tag does not affect enzyme activity or binding
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operons HdrED, hdrD2, hdrA1C1B1, and hdrA2C2B2 with a putative polyferredoxin, several hdr alleles are present in the Methanosarcina acetivorans C2A chromosome, phylogenetic analysis
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overexpression of HdrB subunit in Bacillus subtilis
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subunit HdrB is produced in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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