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2-(methylthio)ethanesulfonic acid reductase
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Coenzyme-B sulfoethylthiotransferase alpha
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Coenzyme-B sulfoethylthiotransferase beta
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Coenzyme-B sulfoethylthiotransferase gamma
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methyl coenzyme M reductase
methyl coenzyme M reductase A
methyl coenzyme M reductase I
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methyl coenzyme-M reductase
Methanogenic bacterium
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methyl-coenzyme M reductase
methyl-coenzyme M reductase A
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methyl-coenzyme-M reductase
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methylcoenzyme M reductase
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S-methyl-coenzyme M reductase
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MaMCR
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MCR
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MCR
Candidatus Polytropus marinifundus
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MCR
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661554, 662467, 662468, 672069, 672222, 673602, 674934, 690930, 692745, 693265, 693838, 702287, 704208, 724146, 724279, 725201, 738676, 762394
MCR I
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isoform
MCR II
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isoform
mcrA
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gene name, encoding subunit A
mcrA
Candidatus Polytropus marinifundus
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mcrA
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gene name, encoding subunit A
mcrA
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gene name, encoding subunit A
mcrA
Methanocellales RC-I
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mcrB
Candidatus Polytropus marinifundus
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mcrG
Candidatus Polytropus marinifundus
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MCRok
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methyl coenzyme M reductase
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methyl coenzyme M reductase
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methyl coenzyme M reductase
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methyl coenzyme M reductase
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methyl coenzyme M reductase
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
Methanocellales RC-I
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl coenzyme M reductase A
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
Candidatus Polytropus marinifundus
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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661554, 662467, 662468, 662469, 672069, 672222, 673602, 674693, 674934, 690930, 692745, 693838, 702287, 704208, 724146, 724279, 725201, 737451, 738676, 762394
methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
UniProt
methyl-coenzyme M reductase
UniProt
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methyl-coenzyme M reductase
UniProt
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methyl-coenzyme M reductase
UniProt
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methyl-coenzyme M reductase
methanotrophic archaeon
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-coenzyme M reductase
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methyl-CoM reductase
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methyl-ScoM reductase
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methyl-ScoM reductase
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methyl-ScoM reductase
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methyl-ScoM reductase
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methyl-ScoM reductase
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MMP1559
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methyl-CoM + CoB = CoM-S-S-CoB + methane
methyl-CoM + CoB = CoM-S-S-CoB + methane
proposed reaction mechanism uses a radical intermediate and a nickel organic compound. Suggested solutions for enzyme state, structure, reaction cycle and binding mechanism for the enzyme are given
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methyl-CoM + CoB = CoM-S-S-CoB + methane
ternary complex type
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methyl-CoM + CoB = CoM-S-S-CoB + methane
methylreductase complex mechanism suggested
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methyl-CoM + CoB = CoM-S-S-CoB + methane
the enzyme from methanogenic bacteria requires the hydroprophinoid nickel complex coenzyme F-430. Highly specific for coenzyme B with a heptanoyl chain
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methyl-CoM + CoB = CoM-S-S-CoB + methane
ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen
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methyl-CoM + CoB = CoM-S-S-CoB + methane
in the active site region of both isozymes, five modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271
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methyl-CoM + CoB = CoM-S-S-CoB + methane
in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271
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methyl-CoM + CoB = CoM-S-S-CoB + methane
in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271
methyl-CoM + CoB = CoM-S-S-CoB + methane
in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271
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methyl-CoM + CoB = CoM-S-S-CoB + methane
in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, and 1-N-methylhistidine alpha257
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methyl-CoM + CoB = CoM-S-S-CoB + methane
in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, and 5-(S)-methylarginine alpha271
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methyl-CoM + CoB = CoM-S-S-CoB + methane
mechanism, nucleophilic attack of Ni(I)-MCRred1 on the methyl group of methyl-SCoM generates a methyl-Ni intermediate
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methyl-CoM + CoB = CoM-S-S-CoB + methane
two possible catalytic mechanisms, overview
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methyl-CoM + CoB = CoM-S-S-CoB + methane
reaction mechanism, different varaints, the Ni(I) center is assumed to attack the thioether sulfur of CH3-S-CoM, generating -CH3 and the thiolate complex CoM-SNi(II)F430 as intermediates, detailed overview
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methyl-CoM + CoB = CoM-S-S-CoB + methane
Two reaction mechanisms for methane formation distinguishable by the first step of catalysis, overview
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methyl-CoM + CoB = CoM-S-S-CoB + methane
catalytic mechanism, the first step of the mechanism is proposed to involve a nucleophilic attack of the NiI active state, MCRred1, on Me-SCoM to form a NiIII-methyl intermediate, spectroscopic analysis and structures, overview
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methyl-CoM + CoB = CoM-S-S-CoB + methane
the first step of the mechanism is proposed to involve a nucleophilic attack of the NiI active state, MCRred1, on Me-SCoM to form a NiIII-methyl intermediate, spectroscopic analysis and structures, overview
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methyl-CoM + CoB = CoM-S-S-CoB + methane
radical mechanism of biological methane synthesis by methyl-coenzyme M reductase, overview. Transient kinetic, spectroscopic [ultraviolet-visible (UV-Vis), EPR, and MCD], and computational studies of the first step in the MCR catalytic mechanism are performed to trap and identify the key intermediates that differ between proposed mechanisms I and II
methyl-CoM + CoB = CoM-S-S-CoB + methane
the proposed mechanism for methane oxidation by MCR initiates with the attack of an F430-Ni(I) species onto the sulfur of methyl-CoM, inducing the homolytic cleavage of the C-S bond and formation of a methyl radical and an F430-Ni(II)-thiolate(CoM) intermediate (step 1). The nascent methyl radical abstracts a hydrogen atom from the CoB thiol, generating methane and a CoB thiyl radical (step 2). The CoB thiyl radical attacks the sulfur of the F430-Ni(II)-thiolate(CoM) intermediate, affording an F430-Ni(I) species and releasing a CoB/CoM heterodisulfide (CoB-S-S-CoM) (step 3). The addition of CoB and methyl-CoM to this form of the enzyme allows for another round of turnover (step 4). It is likely that the same mechanism proposed for MCR can be used for ethane and even additional short-chain alkanes such as propane and butane. MCR converts ethane to ethyl-CoM rather than methane to methyl-CoM
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methyl-CoM + CoB = CoM-S-S-CoB + methane
the reaction proceeds via an unprecedented methyl radical intermediate
methyl-CoM + CoB = CoM-S-S-CoB + methane
the reaction proceeds via an unprecedented methyl radical intermediate
methyl-CoM + CoB = CoM-S-S-CoB + methane
the reaction proceeds via an unprecedented methyl radical intermediate
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methyl-CoM + CoB = CoM-S-S-CoB + methane
the reaction proceeds via an unprecedented methyl radical intermediate
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methyl-CoM + CoB = CoM-S-S-CoB + methane
ternary complex type
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methyl-CoM + CoB = CoM-S-S-CoB + methane
the reaction proceeds via an unprecedented methyl radical intermediate
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methyl-CoM + CoB = CoM-S-S-CoB + methane
the reaction proceeds via an unprecedented methyl radical intermediate
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methyl-CoM + CoB = CoM-S-S-CoB + methane
the reaction proceeds via an unprecedented methyl radical intermediate
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
2-(methylthio)ethansulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
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i.e. CoM and CoB
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
CH3-S-CoM + HS-CoB6
CoM-S-S-CoB6 + methane
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i.e. N-7-mercaptohexanoylthreonine phosphate
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CH3-S-CoM + HS-CoB8
CoM-S-S-CoB8 + methane
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a two-electron transfer reaction
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CH3-S-CoM + HS-CoB9
CoM-S-S-CoB9 + methane
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CH3-S-CoM + SH-CoB
CoM-S-S-CoB + methane
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
CH3-S-CoM + SH-CoB8
CoM-S-S-CoB8 + methane
CH3-S-CoM + SH-CoB9
CoM-S-S-CoB9 + methane
CH3-S-CoM3 + HS-CoB8
CoM3-S-S-CoB8 + methane
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CoM-S-S-CoB + methane
methyl-CoM + CoB
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ethyl coenzyme M + coenzyme B
ethane + CoM-S-S-CoB
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1% of the activity with methyl coenzyme M
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ethyl-CoM + CoB
CoM-S-S-CoB + ethane
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methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoB-S-S-CoM
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i.e. methyl-SCoM
a the mixed disulfide
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methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
methyl-CoM + CoB
CoM-S-S-CoB + methane
methylmercaptopropionate + HS-CoB
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is about 110fold less reactive than the natural substrate methyl-SCoM
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additional information
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2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
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i.e. CoM and CoB
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2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
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i.e. CoM and CoB, the enzyme exists in the the inactive Ni(II) MCRox1-silent form and the active Ni(I) MCRred1 form with transition from MCRred1 to MCRred2 forms, the protein is able to undergo a conformational change upon binding of the second substrate. Analysis of the catalytic mechanism of the reduction at the nickel center using inhibitory fluorescent trifluoromethyl thio esters of the substrate CoB for spectroscopic analysis of the structure of the enzyme-cofactor complex, derivatives synthesis, overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR catalyzes the methane-forming step in methanogenic archaea
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR catalyzes the methane-forming step in methanogenic archaea
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR catalyzes the methane-forming step in methanogenic archaea
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
MCR catalyzes the methane-forming step in methanogenic archaea
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR catalyzes the methane-forming step in methanogenic archaea
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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i.e. methyl-coenzyme M + coenzyme B
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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key step in the convertion of C1 substrates or acetate to methane thereby providing energy for the cell
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR catalyzes the first proposed step in anaerobic methane oxidation and terminal step in methanogenesis by using N-7-mercaptoheptanolyl-threonine phosphate, i.e. CoB-SH. as the two-electron donor to reduce 2-(methylthiol)-ethane sulfonate, i.e. methyl-SCoM, to methane, and producing the heterodisulfide, CoBS-SCoM
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR catalyzes the methane-forming step in methanogenic archaea
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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catalytic cycle and proton transfer mechanism and energetics, reaction complex formations and mechanism, detailed overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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i.e. methyl-coenzyme M + coenzyme B, selectivity of the MCR reaction toward nucleophilic attack by Ni(I)
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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i.e. methyl-coenzyme M or 2-methylmercaptoethanesulfonate + coenzyme B or N-7-mercaptoheptanoylthreonine phosphate
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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the active enzyme is in the MCRred1c form, coordinated ligands of the two paramagnetic MCRred2 states, reduction and oxidation states and critical bond activation step, detailed overview
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
HS-CoB is N-(7-mercaptoheptanoyl)-L-threonine 3-O-phosphate
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?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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i.e. N-7-mercaptoheptanoylthreonine phosphate, Ni(III)-methyl is an intermediate in methane formation
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?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
HS-CoB is N-(7-mercaptoheptanoyl)-L-threonine 3-O-phosphate
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?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
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r
CH3-S-CoM + SH-CoB
CoM-S-S-CoB + methane
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CH3-S-CoM + SH-CoB
CoM-S-S-CoB + methane
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CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
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CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
i.e. N-5-mercaptopentanoylthreonine phosphate
2.8.4.1 coenzyme-B sulfoethylthiotransferase
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