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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
-
i.e. CoM and CoB
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
CH3-S-CoM + HS-CoB6
CoM-S-S-CoB6 + methane
-
i.e. N-7-mercaptohexanoylthreonine phosphate
-
-
?
CH3-S-CoM + HS-CoB8
CoM-S-S-CoB8 + methane
-
a two-electron transfer reaction
-
-
?
CH3-S-CoM + HS-CoB9
CoM-S-S-CoB9 + methane
-
-
-
-
?
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
-
-
-
-
?
CoM-S-S-CoB + methane
methyl-CoM + CoB
-
-
-
-
?
ethyl coenzyme M + coenzyme B
ethane + CoM-S-S-CoB
-
1% of the activity with methyl coenzyme M
-
-
?
ethyl-CoM + CoB
CoM-S-S-CoB + ethane
-
-
-
-
?
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
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
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
?
-
is about 110fold less reactive than the natural substrate methyl-SCoM
-
-
?
additional information
?
-
2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
-
i.e. CoM and CoB
-
-
?
2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
-
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR catalyzes the methane-forming step in methanogenic archaea
-
-
?
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR catalyzes the methane-forming step in methanogenic archaea
-
-
?
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR catalyzes the methane-forming step in methanogenic archaea
-
-
?
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
MCR catalyzes the methane-forming step in methanogenic archaea
-
-
?
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR catalyzes the methane-forming step in methanogenic archaea
-
-
?
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
-
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. methyl-coenzyme M + coenzyme B
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
key step in the convertion of C1 substrates or acetate to methane thereby providing energy for the cell
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR catalyzes the methane-forming step in methanogenic archaea
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
catalytic cycle and proton transfer mechanism and energetics, reaction complex formations and mechanism, detailed overview
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. methyl-coenzyme M + coenzyme B, selectivity of the MCR reaction toward nucleophilic attack by Ni(I)
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. methyl-coenzyme M or 2-methylmercaptoethanesulfonate + coenzyme B or N-7-mercaptoheptanoylthreonine phosphate
-
-
?
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
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
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
HS-CoB is N-(7-mercaptoheptanoyl)-L-threonine 3-O-phosphate
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. N-7-mercaptoheptanoylthreonine phosphate, Ni(III)-methyl is an intermediate in methane formation
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
HS-CoB is N-(7-mercaptoheptanoyl)-L-threonine 3-O-phosphate
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
-
-
r
CH3-S-CoM + SH-CoB
CoM-S-S-CoB + methane
-
-
-
-
?
CH3-S-CoM + SH-CoB
CoM-S-S-CoB + methane
-
-
-
-
?
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
-
-
-
-
?
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
i.e. N-5-mercaptopentanoylthreonine phosphate
-
-
?
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
-
-
-
-
?
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
i.e. N-5-mercaptopentanoylthreonine phosphate
-
-
?
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
i.e. N-6-mercaptohexanoylthreonine phosphate, slow substrate
-
-
?
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
-
methanogenesis occurs 1000fold more slowly than with SH-CoB
-
-
?
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
-
methanogenesis occurs 1000fold more slowly than with SH-CoB
-
-
?
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
i.e. N-6-mercaptohexanoylthreonine phosphate, slow substrate
-
-
?
CH3-S-CoM + SH-CoB8
CoM-S-S-CoB8 + methane
i.e. N-8-mercaptooctanoylthreonine phosphate
-
-
?
CH3-S-CoM + SH-CoB8
CoM-S-S-CoB8 + methane
i.e. N-8-mercaptooctanoylthreonine phosphate
-
-
?
CH3-S-CoM + SH-CoB9
CoM-S-S-CoB9 + methane
i.e. N-9-mercaptononanoylthreonine phosphate
-
-
?
CH3-S-CoM + SH-CoB9
CoM-S-S-CoB9 + methane
i.e. N-9-mercaptononanoylthreonine phosphate
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
key enzyme in methane formation by methanogenic Archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
the enzyme catalyzes the final step in methanogenesis
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
the enzyme is essential in Methanosarcina acetivorans C2A
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
the enzyme catalyzes the final step in methanogenesis
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
the enzyme catalyzes the final step in methanogenesis
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
discussion of mechanism
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
methanogenesis
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
strictly anaerobic conditions
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
reductive methylation
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
rate limiting step in methanogenesis
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
energy metabolism of all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
energy metabolism of all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
key enzyme in methane formation by methanogenic Archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
the enzyme catalyzes the final step in methanogenesis
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
reductive methylation
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
methanogenesis
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
rate limiting step in methanogenesis
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
energy metabolism of all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
energy metabolism of all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
final step in methane formation in all methanogenic archaea
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
methane formation only under H2 not under N2 atmosphere. ATP and FAD also required. Ti(III) citrate can be used as electron source under N2 atmosphere. Dithiothreitol and cyanocobalamin under H2 can also be used for methanogenesis
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
in presence of H2 as source of electrons, requires Mg2+ and catalytic ATP
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
specific for L-enantiomer of coenzyme B
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
methane formation only under H2 not under N2 atmosphere. ATP and FAD also required. Ti(III) citrate can be used as electron source under N2 atmosphere. Dithiothreitol and cyanocobalamin under H2 can also be used for methanogenesis
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
specific for L-enantiomer of coenzyme B
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
Methanocellales RC-I
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
r
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
r
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
r
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
the enzyme is highly specific for methyl-coenzyme M
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
r
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
r
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
additional information
?
-
-
role of methyl-coenzyme M reductase in the anaerobic functionalization of alkanes. Enzyme MCR uses three cofactors to perform the reaction: CoM, coenzyme B (CoB), and a Ni-containing tetrapyrrole, F430
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-
-
additional information
?
-
-
several bifunctional substrates tested, substrates contain both an aliphatic thiol and a methyl thioether function
-
-
?
additional information
?
-
-
MCR also appears to initiate anaerobic methane oxidation, the reverse methanogenesis
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step in methane biosynthesis by methanogenic archaea
-
-
?
additional information
?
-
-
the enzyme catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea
-
-
?
additional information
?
-
-
conversion of MCRox1 toMCRred1 by Ti(III)citrate, bromopropanesulfonate is an alternative substrate of MCR in an ionic reaction that is coenzyme B-independent and leads to debromination of bromopropanesulfonate and formation of a distinct state with an EPR signal that is assigned to a Ni(III)-propylsulfonate species, propanesulfonate formation also occurs in steady-state reactions in the presence of Ti(III) citrate
-
-
?
additional information
?
-
-
the enzyme performs reactions with brominated acid, 4-bromobutyric acid to 16-bromohexadecanoic acid, analogously to the reaction of MCRred1, the active Ni(I)-F430 containing enzyme form, to generate a methyl-Ni(III) intermediate in methane formation with the natural substrate, methyl-SCoM, substrate specificity and acivities, overview
-
-
?
additional information
?
-
-
MCR catalyzes the final step in the biological synthesis of methane. Using coenzyme B, CoBSH, as the two-electron donor, MCR reduces methyl-coenzyme M, methyl-SCoM, to methane and the mixed disulfide, CoB-S-S-CoM. MCR contains coenzyme F430, an essential redox-active nickel tetrahydrocorphin, at its active site. The active form of MCR, MCRred1, contains Ni(I)-F430
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-
?
additional information
?
-
-
MCR reduction/oxidation state, electron paramagnetic resonance status analysis, detailed overview
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-
?
additional information
?
-
-
MCR substrate specificity and reactivation activity of different thiols, e.g. 2-mercaptoethanol, DTT, Na2S, and cysteine, kinetics, overview
-
-
?
additional information
?
-
-
three general mechanisms for the catalytic production of methane by MCR: (1) the Ni-Me/Ragsdale pathway, (2) the Ni-Me/Thauer pathway, (3) the methyl radical pathway. Density functional calculations and electronic-structure calculations and analysis by computational methods, homolytic Ni-S/Ni-C bonds energies, overview
-
-
?
additional information
?
-
-
MCR is the key enzyme in methane formation by methanogenic Archaea. It converts the thioether methyl-coenzyme M and the thiol coenzyme B into methane and the heterodisulfide of coenzyme M and coenzyme B
-
-
?
additional information
?
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-
The active form of the enzyme, referred to as MCRred1, features the tetracoordinate dx2y2 nickel(I) state of the cofactor, simulations of enzyme nickel intermediate states in synthetic complexes, mechanism and modeling, pyriporphyrin-based model and isoporphyrin-based model, overview
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-
?
additional information
?
-
-
no activity with SH-CoB8 or SH-CoB9
-
-
?
additional information
?
-
the substrates bind inside a deep substrate channel with CoBSH nearer to the surface, stretching toward methyl-SCoM, which is close to F430
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-
-
additional information
?
-
-
no activity with SH-CoB8 or SH-CoB9
-
-
?
additional information
?
-
-
dual requirement for electron donors
-
-
?
additional information
?
-
-
ability of the hydrogenase to reduce a number of artificial and naturally occurring electron acceptors is examined
-
-
?
additional information
?
-
-
dual requirement for electron donors
-
-
?
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coenzyme F430
-
-
coenzyme F430
-
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
coenzyme F430
-
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
coenzyme F430
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
coenzyme F430
-
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
coenzyme F430
-
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
coenzyme F430
-
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
coenzyme F430
-
a redox-active nickel tetrahydrocorphin bound at the active site, contains low-spin Ni(II), determination of the cofactor reduction site at the exocyclic ketone group by NMR study, mass spectrometry, and QM/MM computations, conversion of F430 to F330 reduces the hydrocorphin ring but not the metal, reduction of F430 with Ti(III) citrate to generate F380, corresponding to the active MCRred1 state, reduces the Ni(II) to Ni(I) but does not reduce the tetrapyrrole ring system, overview
coenzyme F430
-
an essential redox-active nickel tetrahydrocorphin, bound at the active site, the active form of MCR, MCRred1, contains Ni(I)-F430
coenzyme F430
-
each active site has the nickel porphyrinoid F430 as a prosthetic group, in the active state, F430 contains the transition metal in the Ni(I) oxidation state
coenzyme F430
-
structure analysis using crystal structure PDB code 1MRO, and conformational changes during catalysis, free cofactor F430 is thermally unstable, it first epimerizes to 13-epi F430 and then in a second epimerization to 12,13-diepi F430, nonplanar deformations, overview
coenzyme F430
-
the nickel-containing tetrapyrrole is essential for the reaction, and is bound to the active site
F-430
-
-
F-430
-
1.6-1.8 mol F-430/mol enzyme
F-430
-
contains two tightly bound molecules of coenzyme F-430
F-430
-
the extracted form in aqueous solution and protein-bound form are studied by using low-temperature magnetic-circular-dichroism spectroscopy. Tightly bound nickel tetrapyrrole cofactor
F-430
-
nickel porphinoid coenzyme M
F-430
-
2 mol coenzyme F-430/mol enzyme
F-430
-
2 mol nickel porphinoid/mol enzyme, prosthetic group
F-430
-
1 mol coenzyme F-430/mol enzyme
F-430
-
cofactor F430 undergoes a significant conformational change when it binds to the enzyme. Conversion from MCRox1 to MCRred1 involves major conformational rearrangements, which are propose to be due to a 2-electron reversible reduction of the hydrocorphin ring of F430
F-430
-
nickel-containing porphinoid cofactor F-430. Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms
F-430
-
prosthetic group has to be in the Ni(I) oxidation state for the enzyme to be active
F-430
-
tightly bound nickel porphinol. The enzyme is active only when its prosthetic group in in the NI(I)-reduced state
F-430
-
active in Ni(I) oxidation state, inactive in Ni(II) state, binding structure and oxidation states, hyperfine interactions of protons, detailed overview
F-430
-
binding structure, and different oxidation states F430 (Ni(I)/Ni(II)/Ni(III)), Ni(I) is the active state, overview
F-430
-
nickel corphin coenzyme F430, structure of the free coenzyme, overview
F-430
-
the active site of MCR includes a noncovalently bound Ni tetrapyrrolic coenzyme F430, which is in the Ni(I) state in the active enzyme, MCRred1
F-430
-
the enzyme has two structurally interlinked active sites embedded in an alpha2beta2gamma2 subunit structure. Each active site has the nickel porphyrinoid F430 as a prosthetic group. In the active state, F430 contains the transition metal in the Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state
F-430
with Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state, selectivity of the MCR reaction toward nucleophilic attack by Ni(I)
F-430
-
a nickel hydrocorphin coenzyme F430, the Ni(I) MCRred1 form and the inactive Ni(II) MCRox1-silent form, no formation of an MCRis dependent methyl-Ni(F430) species, 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
F-430
-
an active site Ni cofactor
F-430
-
the Ni-F430 cofactor is bound to the active site and exists in two oxidation states
F-430
-
the active site of the enzyme contains an essential redox-active nickel tetrapyrrole cofactor, coenzyme F430, which is active in the Ni(I) state
F-430
the enzyme contains the highly reduced nickel-tetrapyrrole coenzyme F430
F-430
the enzyme contains the Ni porphinoid F430 as prosthetic group
F-430
the enzyme molecule contains two mol of the nickel porphinoid factor 430 non-covalently bound. The nickel center of F430 is coordinated by the coenzyme M sulfhydryl group from one side and by the oxygen atom of a glutamine side-chain from the other
F-430
coenzyme F430, during enzymatic catalysis, the Ni(I) of coenzyme F430 seen to attack the sulfur atom of methyl coenzyme M, producing a methyl radical intermediate
F-430
coenzyme F430, MCR is a unique enzyme and of great intrinsic interest. The prosthetic group is the first known naturally occurring nickel tetrapyrrole, coenzyme F430. For the enzyme to be active, the metal must be in the Ni(I) oxidation state. Because the redox potential of the F430Ni(II)/F430Ni(I) couple is near -650 mV, the stability of the Ni(I) prosthetic group is critical for maintaining enzyme activity
F-430
-
coenzyme F430, rapid kinetic studies rule out methyl-Ni(III) and trap the MCRox1-silent intermediate. Identification of an MCRox1-like state, specifically a F430-Ni(III)-SCoM/CoBS- intermediate, from direct DFT calculations
F-430
coenzyme F430, rapid kinetic studies rule out methyl-Ni(III) and trap the MCRox1-silent intermediate. Identification of an MCRox1-like state, specifically a F430-Ni(III)-SCoM/CoBS- intermediate, from direct DFT calculations
F-430
-
coenzyme F430, rapid kinetic studies rule out methyl-Ni(III) and trap the MCRox1-silent intermediate. Identification of an MCRox1-like state, specifically a F430-Ni(III)-SCoM/CoBS- intermediate, from direct DFT calculations
F-430
-
coenzyme F430, rapid kinetic studies rule out methyl-Ni(III) and trap the MCRox1-silent intermediate. Identification of an MCRox1-like state, specifically a F430-Ni(III)-SCoM/CoBS- intermediate, from direct DFT calculations
additional information
-
2 molecules of the nickel porphinoid coenzyme F-430 are embedded between the subunits, forming 2 structurally identical active sites
-
additional information
-
enzyme consists of 2 symmetry-equivalent active sites containing one molecule of the hydroporphinoid nickel complex coenzyme F-430, enzyme is active only if the metal center of coenzyme F-430 is in the nickel(I) form
-
additional information
-
enzyme MCR uses three cofactors to perform the reaction: CoM, coenzyme B (CoB), and a Ni-containing tetrapyrrole, F430
-
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evolution
-
analysis of mcr-containing archaeal metagenome-assembled genomes (MAGs) from several hot springs, phylogenetic analysis, and evolution of methyl-coenzyme M reductase-containing hot spring Archaea, overview. A hydrothermal origin for these microorganisms is predicted based on optimal growth temperature predictions. Methane/alkane oxidation or methanogenesis at high temperature likely existed in a common archaeal ancestor
evolution
-
analysis of mcr-containing archaeal metagenome-assembled genomes (MAGs) from several hot springs, phylogenetic analysis, and evolution of methyl-coenzyme M reductase-containing hot spring Archaea, overview. A hydrothermal origin for these microorganisms is predicted based on optimal growth temperature predictions. Methane/alkane oxidation or methanogenesis at high temperature likely existed in a common archaeal ancestor
evolution
-
analysis of mcr-containing archaeal metagenome-assembled genomes (MAGs) from several hot springs, phylogenetic analysis, and evolution of methyl-coenzyme M reductase-containing hot spring Archaea, overview. A hydrothermal origin for these microorganisms is predicted based on optimal growth temperature predictions. Methane/alkane oxidation or methanogenesis at high temperature likely existed in a common archaeal ancestor
evolution
-
analysis of mcr-containing archaeal metagenome-assembled genomes (MAGs) from several hot springs, phylogenetic analysis, and evolution of methyl-coenzyme M reductase-containing hot spring Archaea, overview. A hydrothermal origin for these microorganisms is predicted based on optimal growth temperature predictions. Methane/alkane oxidation or methanogenesis at high temperature likely existed in a common archaeal ancestor
evolution
-
analysis of mcr-containing archaeal metagenome-assembled genomes (MAGs) from several hot springs, phylogenetic analysis, and evolution of methyl-coenzyme M reductase-containing hot spring Archaea, overview. A hydrothermal origin for these microorganisms is predicted based on optimal growth temperature predictions. Methane/alkane oxidation or methanogenesis at high temperature likely existed in a common archaeal ancestor. Five mcr-containing MAGs are identified as Verstraetearchaeota
evolution
-
the marker gene for anaerobic methane cycling (mcrA) is more widespread in the Archaea than previously thought. Small-subunit (SSU) rRNA gene analyses indicate that Bathyarchaeota are predominant in seven of ten sediment layers, while the Verstraetearchaeota and Euryarchaeota occur in lower relative abundance. Targeted amplification of mcrA genes suggests that diverse taxa contribute to alkane cycling in geothermal environments. Two deeply-branching mcrA clades related to Bathyarchaeota are identified, while highly abundant verstraetearchaeotal mcrA sequences are also recovered. SSU rRNA gene survey of Archaea and phylogenetic analysis and distribution, overview
evolution
-
the marker gene for anaerobic methane cycling (mcrA) is more widespread in the Archaea than previously thought. Small-subunit (SSU) rRNA gene analyses indicate that Bathyarchaeota are predominant in seven of ten sediment layers, while the Verstraetearchaeota and Euryarchaeota occur in lower relative abundance. Targeted amplification of mcrA genes suggests that diverse taxa contribute to alkane cycling in geothermal environments. Two deeply-branching mcrA clades related to Bathyarchaeota are identified, while highly abundant verstraetearchaeotal mcrA sequences are also recovered. SSU rRNA gene survey of Archaea and phylogenetic analysis and distribution, overview
evolution
-
the marker gene for anaerobic methane cycling (mcrA) is more widespread in the Archaea than previously thought. Small-subunit (SSU) rRNA gene analyses indicate that Bathyarchaeota are predominant in seven of ten sediment layers, while the Verstraetearchaeota and Euryarchaeota occur in lower relative abundance. Targeted amplification of mcrA genes suggests that diverse taxa contribute to alkane cycling in geothermal environments. Two deeply-branching mcrA clades related to Bathyarchaeota are identified, while highly abundant verstraetearchaeotal mcrA sequences are also recovered. SSU rRNA gene survey of Archaea and phylogenetic analysis and distribution, overview
evolution
Candidatus Polytropus marinifundus
-
the number of archaeal clades encoding the MCR continues to grow, suggesting that this complex is inherited from an ancient ancestor, or has undergone extensive horizontal gene transfer, detailed phylogenetic analysis and tree, overview. Candidatus Polytropus marinifundus gen. nov. sp. nov. encodes two divergent McrABG operons similar to those found in Candidatus Bathyarchaeota and Candidatus Syntrophoarchaeum metagenome-assembled genomes (MAGs). The Ca. P. marinifundus MCR operons are horizontally transferred
malfunction
growth defects associated with loss of the McrA thioglycine modification. The DELTAycaO-tfuA mutant lacks the McrA Gly465 thioamide
malfunction
methylation mutant Mko4551 shows impaired growth under stress conditions
malfunction
-
growth defects associated with loss of the McrA thioglycine modification. The DELTAycaO-tfuA mutant lacks the McrA Gly465 thioamide
-
malfunction
-
methylation mutant Mko4551 shows impaired growth under stress conditions
-
malfunction
-
growth defects associated with loss of the McrA thioglycine modification. The DELTAycaO-tfuA mutant lacks the McrA Gly465 thioamide
-
malfunction
-
methylation mutant Mko4551 shows impaired growth under stress conditions
-
malfunction
-
growth defects associated with loss of the McrA thioglycine modification. The DELTAycaO-tfuA mutant lacks the McrA Gly465 thioamide
-
malfunction
-
methylation mutant Mko4551 shows impaired growth under stress conditions
-
metabolism
-
MCR catalyzes the terminal step in the formation of biological methane from methyl-coenzyme M and coenzyme B
metabolism
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
metabolism
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
metabolism
-
the enzyme catalyzes the final step of methanogenesis in Methanobrevibacter ruminantium
metabolism
-
the enzyme catalyzes the final step in methanogenesis
metabolism
-
MCR is the terminal enzyme in methanogenesis (or the first in anaerobic methane oxidation, AOM) and is responsible for the release of methane. Unlike in methanotrophic archaea, Candidatus Argoarchaeum ethanivorans contains a homologue of N5, N10-methylenetetrahydromethanopterin reductase (Mer) and the membrane-associated heterodisulfide reductase. In particular, the heterodisulfide reductase makes it possible for the MCR reaction to be reversible, allowing for the anaerobic oxidation of methane and other short-chain alkanes
metabolism
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
metabolism
-
overview of metabolic potentials in mcr-containing MAGs
metabolism
-
overview of metabolic potentials in mcr-containing MAGs
metabolism
-
overview of metabolic potentials in mcr-containing MAGs
metabolism
-
overview of metabolic potentials in mcr-containing MAGs
metabolism
-
overview of metabolic potentials in mcr-containing MAGs
metabolism
the last and methane-releasing step of methanogenesis is catalysed by the enzyme methyl-coenzyme M reductase (MCR)
metabolism
-
the last and methane-releasing step of methanogenesis is catalysed by the enzyme methyl-coenzyme M reductase (MCR)
-
metabolism
-
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
-
metabolism
-
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
metabolism
-
the last and methane-releasing step of methanogenesis is catalysed by the enzyme methyl-coenzyme M reductase (MCR)
-
metabolism
-
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
-
metabolism
-
the last and methane-releasing step of methanogenesis is catalysed by the enzyme methyl-coenzyme M reductase (MCR)
-
metabolism
-
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
metabolism
-
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
-
physiological function
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
physiological function
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
physiological function
-
MCR is the terminal enzyme in methanogenesis (or the first in anaerobic methane oxidation, AOM) and is responsible for the release of methane. MCR converts ethane to ethyl-CoM rather than methane to methyl-CoM. The ethyl-CoM is hypothesized to be oxidized to CO2 via reverse methanogenesis
physiological function
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
physiological function
methyl-coenzyme M reductase is a key enzyme in methanogenic and methanotrophic Archaea. Methyl-coenzyme M reductase (MCR) is a unique enzyme found exclusively in anaerobic archaea, where it catalyzes the reversible conversion of methyl-coenzyme M (CoM, 2-methylmercaptoethane-sulfonate) and coenzyme B (CoB, 7-thioheptanoylthreoninephosphate) to methane and a CoB-CoM heterodisulfide. The activity plays a critical role in the global carbon cycle
physiological function
methyl-coenzyme M reductase is a key enzyme in methanogenic and methanotrophic Archaea. Methyl-coenzyme M reductase (MCR) is a unique enzyme found exclusively in anaerobic archaea, where it catalyzes the reversible conversion of methyl-coenzyme M (CoM, 2-methylmercaptoethane-sulfonate) and coenzyme B (CoB, 7-thioheptanoylthreoninephosphate) to methane and a CoB-CoM heterodisulfide. The activity plays a critical role in the global carbon cycle
physiological function
roles of Mcr in the global carbon cycle. CH4 is an important biofuel as well as a potential feedstock for the chemical industry if it can be converted by Mcr to a liquid biofuel with a high energy density. CH4 is also a potent greenhouse gas, increases of which are contributing to global warming
physiological function
-
the enzyme is involved in anaerobic alkane cycling
physiological function
-
the enzyme is involved in anaerobic alkane cycling
physiological function
-
the enzyme is involved in anaerobic alkane cycling
physiological function
the enzyme that catalyzes the chemical step of methane synthesis or oxidation is methyl-coenzyme M reductase (MCR), which contains a nickel hydrocorphinate F430 at its active site. This reaction involves conversion of the methyl donor, methylcoenzyme M (methyl-SCoM), and the electron donor, coenzyme B (CoBSH, N-7-mercaptoheptanoylthreonine phosphate), to methane and the mixed disulfide CoBS-SCoM
physiological function
Candidatus Polytropus marinifundus
-
the methyl-coenzyme M reductase (MCR) complex is a key enzyme in archaeal methane generation and has been proposed to also be involved in the oxidation of short-chain hydrocarbons including methane, butane, and potentially propane
physiological function
-
methyl-coenzyme M reductase is a key enzyme in methanogenic and methanotrophic Archaea. Methyl-coenzyme M reductase (MCR) is a unique enzyme found exclusively in anaerobic archaea, where it catalyzes the reversible conversion of methyl-coenzyme M (CoM, 2-methylmercaptoethane-sulfonate) and coenzyme B (CoB, 7-thioheptanoylthreoninephosphate) to methane and a CoB-CoM heterodisulfide. The activity plays a critical role in the global carbon cycle
-
physiological function
-
methyl-coenzyme M reductase is a key enzyme in methanogenic and methanotrophic Archaea. Methyl-coenzyme M reductase (MCR) is a unique enzyme found exclusively in anaerobic archaea, where it catalyzes the reversible conversion of methyl-coenzyme M (CoM, 2-methylmercaptoethane-sulfonate) and coenzyme B (CoB, 7-thioheptanoylthreoninephosphate) to methane and a CoB-CoM heterodisulfide. The activity plays a critical role in the global carbon cycle
-
physiological function
-
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
-
physiological function
-
roles of Mcr in the global carbon cycle. CH4 is an important biofuel as well as a potential feedstock for the chemical industry if it can be converted by Mcr to a liquid biofuel with a high energy density. CH4 is also a potent greenhouse gas, increases of which are contributing to global warming
-
physiological function
-
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
physiological function
-
methyl-coenzyme M reductase is a key enzyme in methanogenic and methanotrophic Archaea. Methyl-coenzyme M reductase (MCR) is a unique enzyme found exclusively in anaerobic archaea, where it catalyzes the reversible conversion of methyl-coenzyme M (CoM, 2-methylmercaptoethane-sulfonate) and coenzyme B (CoB, 7-thioheptanoylthreoninephosphate) to methane and a CoB-CoM heterodisulfide. The activity plays a critical role in the global carbon cycle
-
physiological function
-
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
-
physiological function
-
methyl-coenzyme M reductase is a key enzyme in methanogenic and methanotrophic Archaea. Methyl-coenzyme M reductase (MCR) is a unique enzyme found exclusively in anaerobic archaea, where it catalyzes the reversible conversion of methyl-coenzyme M (CoM, 2-methylmercaptoethane-sulfonate) and coenzyme B (CoB, 7-thioheptanoylthreoninephosphate) to methane and a CoB-CoM heterodisulfide. The activity plays a critical role in the global carbon cycle
-
physiological function
-
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
-
physiological function
-
methyl-coenzyme M reductase is a key enzyme in methanogenic and methanotrophic Archaea. Methyl-coenzyme M reductase (MCR) is a unique enzyme found exclusively in anaerobic archaea, where it catalyzes the reversible conversion of methyl-coenzyme M (CoM, 2-methylmercaptoethane-sulfonate) and coenzyme B (CoB, 7-thioheptanoylthreoninephosphate) to methane and a CoB-CoM heterodisulfide. The activity plays a critical role in the global carbon cycle
-
physiological function
-
methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. The methyl coenzyme M reductase (MCR) is central to all methanogenic pathways. Whether or not methane is formed from CO2, methyl groups, or acetate, the final step is catalyzed by MCR. In this reaction, methyl coenzyme M (CH3-S-CoM) is reduced by the thiol coenzyme B (HS-CoB) to form methane and the mixed disulfide (also called heterodisulfide, CoM-S-S-CoB). MCR is also involved in the anaerobic oxidation of methane
-
additional information
initial steps in three proposed mechanisms of MCR catalysis: (i) mechanism I involves nucleophilic attack of Ni(I)-MCRred1 on the methyl group of methyl-SCoM to generate a methyl-Ni(III) intermediate. This mechanism is similar to that of B12-dependent methyltransferases, which generate a methyl-cob(III) alamin intermediate. (ii) In mechanism II, Ni(I) attack on the sulfur atom of methyl-SCoM promotes the homolytic cleavage of the methyl-sulfur bond to produce a methyl radical and a Ni(II)-thiolate. (iii) Mechanism III involves nucleophilic attack of Ni(I) on the sulfur of methyl-SCoM to form a highly reactive methyl anion and Ni(III)-SCoM (MCRox1)
additional information
ordered assembly model for MCR expression
additional information
the enzyme possesses two identical active sites, each of which contains up to five posttranslationally modified amino acid residues. Role of Mmp10 in Mcr methylation on Arg275 and function in methogenesis,mutational analysis, overview
additional information
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the enzyme possesses two identical active sites, each of which contains up to five posttranslationally modified amino acid residues. Role of Mmp10 in Mcr methylation on Arg275 and function in methogenesis,mutational analysis, overview
additional information
-
ordered assembly model for MCR expression
-
additional information
-
the enzyme possesses two identical active sites, each of which contains up to five posttranslationally modified amino acid residues. Role of Mmp10 in Mcr methylation on Arg275 and function in methogenesis,mutational analysis, overview
-
additional information
-
ordered assembly model for MCR expression
-
additional information
-
ordered assembly model for MCR expression
-
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alkylation
the posttranslational methylation of arginine in methyl coenzyme M reductase has a profound impact on both methanogenesis and growth of Methanococcus maripaludis. Protein Mmp10 is necessary for arginine methylation. Replacement of the only conserved His residue in the C-terminal half of Mmp10 with either G or F results in a loss of less than 1% of Arg275 methylation
alkylation
-
the posttranslational methylation of arginine in methyl coenzyme M reductase has a profound impact on both methanogenesis and growth of Methanococcus maripaludis. Protein Mmp10 is necessary for arginine methylation. Replacement of the only conserved His residue in the C-terminal half of Mmp10 with either G or F results in a loss of less than 1% of Arg275 methylation
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alkylation
enzyme MCR contains methylhistidine (His271) and methylcysteine (Cys472), as well as 5-C-(S)-methylarginine. A unique radical SAM methyltransferase is required for the sp3-C-methylation of the arginine residue of methyl-coenzyme M reductase, the a 5-C-(S)-methylarginine is located close to the active site of the enzyme. Deletion of the methyltransferase gene ma4551 in Methanosarcina acetivorans strain WWM1 leads to the production of an active MCR lacking the C-5-methylation of the respective arginine residue. The methylated arginine is important for MCR stability under stress conditions Identification of potential radical SAM methyltransferase genes in the genomes of methanogens, overview
alkylation
S-methylation of Cys472 in McrA by a SAM-dependent methyltransferase MA4545 or McmA belonging to the InterPro superfamily (UniProt ID Q8THH2). The DELTAmcmA mutant is viable on all growth substrates tested, relative to wild-type, the mutant grows 30% slower on DMS, and a 12% decrease in growth yield is observed on trimethylamine. Even though the S-methylation of Cys472 in McrA is dispensable in Methanosarcina acetivorans, it is clearly important for methanogenic growth on certain substrates. Conversion of Arg285 in McrA to 5-(S)-methylarginine depends on enzyme MamA. The L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA and mcmA, respectively, as well as the didehydroaspartate at Asp470
alkylation
-
S-methylation of Cys472 in McrA by a SAM-dependent methyltransferase MA4545 or McmA belonging to the InterPro superfamily (UniProt ID Q8THH2). The DELTAmcmA mutant is viable on all growth substrates tested, relative to wild-type, the mutant grows 30% slower on DMS, and a 12% decrease in growth yield is observed on trimethylamine. Even though the S-methylation of Cys472 in McrA is dispensable in Methanosarcina acetivorans, it is clearly important for methanogenic growth on certain substrates. Conversion of Arg285 in McrA to 5-(S)-methylarginine depends on enzyme MamA. The L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA and mcmA, respectively, as well as the didehydroaspartate at Asp470
-
alkylation
-
enzyme MCR contains methylhistidine (His271) and methylcysteine (Cys472), as well as 5-C-(S)-methylarginine. A unique radical SAM methyltransferase is required for the sp3-C-methylation of the arginine residue of methyl-coenzyme M reductase, the a 5-C-(S)-methylarginine is located close to the active site of the enzyme. Deletion of the methyltransferase gene ma4551 in Methanosarcina acetivorans strain WWM1 leads to the production of an active MCR lacking the C-5-methylation of the respective arginine residue. The methylated arginine is important for MCR stability under stress conditions Identification of potential radical SAM methyltransferase genes in the genomes of methanogens, overview
-
alkylation
-
S-methylation of Cys472 in McrA by a SAM-dependent methyltransferase MA4545 or McmA belonging to the InterPro superfamily (UniProt ID Q8THH2). The DELTAmcmA mutant is viable on all growth substrates tested, relative to wild-type, the mutant grows 30% slower on DMS, and a 12% decrease in growth yield is observed on trimethylamine. Even though the S-methylation of Cys472 in McrA is dispensable in Methanosarcina acetivorans, it is clearly important for methanogenic growth on certain substrates. Conversion of Arg285 in McrA to 5-(S)-methylarginine depends on enzyme MamA. The L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA and mcmA, respectively, as well as the didehydroaspartate at Asp470
-
alkylation
-
enzyme MCR contains methylhistidine (His271) and methylcysteine (Cys472), as well as 5-C-(S)-methylarginine. A unique radical SAM methyltransferase is required for the sp3-C-methylation of the arginine residue of methyl-coenzyme M reductase, the a 5-C-(S)-methylarginine is located close to the active site of the enzyme. Deletion of the methyltransferase gene ma4551 in Methanosarcina acetivorans strain WWM1 leads to the production of an active MCR lacking the C-5-methylation of the respective arginine residue. The methylated arginine is important for MCR stability under stress conditions Identification of potential radical SAM methyltransferase genes in the genomes of methanogens, overview
-
alkylation
-
S-methylation of Cys472 in McrA by a SAM-dependent methyltransferase MA4545 or McmA belonging to the InterPro superfamily (UniProt ID Q8THH2). The DELTAmcmA mutant is viable on all growth substrates tested, relative to wild-type, the mutant grows 30% slower on DMS, and a 12% decrease in growth yield is observed on trimethylamine. Even though the S-methylation of Cys472 in McrA is dispensable in Methanosarcina acetivorans, it is clearly important for methanogenic growth on certain substrates. Conversion of Arg285 in McrA to 5-(S)-methylarginine depends on enzyme MamA. The L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA and mcmA, respectively, as well as the didehydroaspartate at Asp470
-
alkylation
-
enzyme MCR contains methylhistidine (His271) and methylcysteine (Cys472), as well as 5-C-(S)-methylarginine. A unique radical SAM methyltransferase is required for the sp3-C-methylation of the arginine residue of methyl-coenzyme M reductase, the a 5-C-(S)-methylarginine is located close to the active site of the enzyme. Deletion of the methyltransferase gene ma4551 in Methanosarcina acetivorans strain WWM1 leads to the production of an active MCR lacking the C-5-methylation of the respective arginine residue. The methylated arginine is important for MCR stability under stress conditions Identification of potential radical SAM methyltransferase genes in the genomes of methanogens, overview
-
side-chain modification
-
methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview
side-chain modification
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methylation of residues in the active site, e.g. at His257, overview
side-chain modification
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methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview
side-chain modification
methylation of residues in the active site, e.g. at His257, overview
side-chain modification
formation of thioglycine (Gly465), growth defects are associated with loss of the McrA thioglycine modification, mutations in ycaO and/or tfuA are responsible for loss of the thioglycine modification. Thioglycine does not influence the global stability of MCR
side-chain modification
the enzyme contains thioglycine (Gly465) and didehydroaspartate (Asp470)
side-chain modification
the L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA (MA0165/MA0164) and mcmA, respectively, as well as the didehydroaspartate at Asp470
side-chain modification
-
the L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA (MA0165/MA0164) and mcmA, respectively, as well as the didehydroaspartate at Asp470
-
side-chain modification
-
formation of thioglycine (Gly465), growth defects are associated with loss of the McrA thioglycine modification, mutations in ycaO and/or tfuA are responsible for loss of the thioglycine modification. Thioglycine does not influence the global stability of MCR
-
side-chain modification
-
the enzyme contains thioglycine (Gly465) and didehydroaspartate (Asp470)
-
side-chain modification
-
the L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA (MA0165/MA0164) and mcmA, respectively, as well as the didehydroaspartate at Asp470
-
side-chain modification
-
formation of thioglycine (Gly465), growth defects are associated with loss of the McrA thioglycine modification, mutations in ycaO and/or tfuA are responsible for loss of the thioglycine modification. Thioglycine does not influence the global stability of MCR
-
side-chain modification
-
the enzyme contains thioglycine (Gly465) and didehydroaspartate (Asp470)
-
side-chain modification
-
the L461-R491 peptide contains the Gly465 and Cys472 that are modified to thioglycine and S-methylcysteine by ycaO-tfuA (MA0165/MA0164) and mcmA, respectively, as well as the didehydroaspartate at Asp470
-
side-chain modification
-
formation of thioglycine (Gly465), growth defects are associated with loss of the McrA thioglycine modification, mutations in ycaO and/or tfuA are responsible for loss of the thioglycine modification. Thioglycine does not influence the global stability of MCR
-
side-chain modification
-
the enzyme contains thioglycine (Gly465) and didehydroaspartate (Asp470)
-
side-chain modification
-
methylation of residues in the active site, e.g. at His257, overview
side-chain modification
-
methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview
additional information
the McrA subunit possesses up to five highly conserved but not universal posttranslational modifications (PTMs) at its active site, including 1-N-methyl-His261, 5-C-(S)-methyl-Arg275, 2-(S)-methyl-Gln403, and thio-Gly448, which are all found within the McrA subunit
additional information
-
the McrA subunit possesses up to five highly conserved but not universal posttranslational modifications (PTMs) at its active site, including 1-N-methyl-His261, 5-C-(S)-methyl-Arg275, 2-(S)-methyl-Gln403, and thio-Gly448, which are all found within the McrA subunit
additional information
-
the McrA subunit possesses up to five highly conserved but not universal posttranslational modifications (PTMs) at its active site, including 1-N-methyl-His261, 5-C-(S)-methyl-Arg275, 2-(S)-methyl-Gln403, and thio-Gly448, which are all found within the McrA subunit
-
additional information
four amino acid modifications are reported to be present in McrA, namely methylhistidine (His271), methylcysteine (Cys472), thioglycine (Gly465) and didehydroaspartate (Asp470). Mass spectrometric analysis
additional information
-
four amino acid modifications are reported to be present in McrA, namely methylhistidine (His271), methylcysteine (Cys472), thioglycine (Gly465) and didehydroaspartate (Asp470). Mass spectrometric analysis
additional information
functional interactions between posttranslationally modified amino acids of methyl-coenzyme M reductase, overview. Modified McrA residues are independently installed
additional information
-
functional interactions between posttranslationally modified amino acids of methyl-coenzyme M reductase, overview. Modified McrA residues are independently installed
additional information
hylogenetic analyses of methyltransferases TfuA and YcaO in methanogenic andmethanotrophic archaea
additional information
-
hylogenetic analyses of methyltransferases TfuA and YcaO in methanogenic andmethanotrophic archaea
additional information
-
functional interactions between posttranslationally modified amino acids of methyl-coenzyme M reductase, overview. Modified McrA residues are independently installed
-
additional information
-
hylogenetic analyses of methyltransferases TfuA and YcaO in methanogenic andmethanotrophic archaea
-
additional information
-
four amino acid modifications are reported to be present in McrA, namely methylhistidine (His271), methylcysteine (Cys472), thioglycine (Gly465) and didehydroaspartate (Asp470). Mass spectrometric analysis
-
additional information
-
functional interactions between posttranslationally modified amino acids of methyl-coenzyme M reductase, overview. Modified McrA residues are independently installed
-
additional information
-
hylogenetic analyses of methyltransferases TfuA and YcaO in methanogenic andmethanotrophic archaea
-
additional information
-
four amino acid modifications are reported to be present in McrA, namely methylhistidine (His271), methylcysteine (Cys472), thioglycine (Gly465) and didehydroaspartate (Asp470). Mass spectrometric analysis
-
additional information
-
functional interactions between posttranslationally modified amino acids of methyl-coenzyme M reductase, overview. Modified McrA residues are independently installed
-
additional information
-
hylogenetic analyses of methyltransferases TfuA and YcaO in methanogenic andmethanotrophic archaea
-
additional information
-
four amino acid modifications are reported to be present in McrA, namely methylhistidine (His271), methylcysteine (Cys472), thioglycine (Gly465) and didehydroaspartate (Asp470). Mass spectrometric analysis
-
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Signor, L.; Knuppe, C.; Hug, R.; Schweizer, B.; Pfaltz, A.; Jaun, B.
Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate-a process mimicking methanogenesis in archaea
Chem. Eur. J.
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3508-3516
2000
Methanobacterium sp.
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Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation
Science
278
1457-1462
1997
Methanothermobacter thermautotrophicus
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Goubeau, M.; Schreiner, G.; Thauer, R.K.
Purified methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F-430 is reduced to the nickel(I) oxidation state by titanium(III) citrate
Eur. J. Biochem.
243
110-114
1997
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
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Properties of the two isoenzymes of methyl-coenzyme M reductase in Methanobacterium thermoautotrophicum
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217
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1993
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
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Substrate-analog-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum
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210
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1992
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
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Methyl-coenzyme M reductase preparations with high specific activity from hydrogen-preincubated cells of Methanobacterium thermoautotrophicum
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291
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1991
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
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Purification and properties of methyl coenzyme M methylreductase from acetate-grown Methanosarcina thermophila
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173
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1991
Methanosarcina thermophila
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Purification and some properties of the methyl-CoM reductase of Methanothrix soehngenii
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1990
Methanothrix soehngenii
-
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The magnetic properties of the nickel cofactor F430 in the enzyme methyl-coenzyme M reductase of Methanobacterium thermoautotrophicum
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260
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1989
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brenda
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Methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum (strain Marburg). Purity, activity and novel inhibitors
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184
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The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg)
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Reductive activation of the methyl coenzyme M methylreductase system of Methanobacterium thermoautotrophicum.DELTA.H
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Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH
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Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium
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Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH
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Methyl coenzyme M reductase from Methanobacterium thermoautotrophicum. Resolution and properties of the components
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Methanosarcina barkeri, Methanobacterium bryantii, Methanobacterium formicicum, Methanothermobacter thermautotrophicus, Methanospirillum hungatei, no activity in Methanobrevibacter ruminantium, no activity in Methanobrevibacter ruminantium M-1
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Identification of methyl coenzyme M reductase A (mcrA) genes associated with methane-oxidizing archaea
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Methanogen diversity evidenced by molecular characterization of methyl coenzyme M reductase A (mcrA) genes in hydrothermal sediments of the Guaymas Basin
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On the mechanism of methyl-coenzyme M reductase
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Methanothermobacter marburgensis
brenda
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X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation
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124
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Methanothermobacter marburgensis
brenda
Harmer, J.; Finazzo, C.; Piskorski, R.; Bauer, C.; Jaun, B.; Duin, E.C.; Goenrich, M.; Thauer, R.K.; Van Doorslaer, S.; Schweiger, A.
Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: A Pulse EPR Study
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127
17744-17755
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Methanothermobacter marburgensis
brenda
Rother, M.; Boccazzi, P.; Bose, A.; Pritchett, M.A.; Metcalf, W.W.
Methanol-dependent gene expression demonstrates that methyl-coenzyme M reductase is essential in Methanosarcina acetivorans C2A and allows isolation of mutants with defects in regulation of the methanol utilization pathway
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187
5552-5559
2005
Methanosarcina acetivorans C2A
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Goenrich, M.; Duin, E.C.; Mahlert, F.; Thauer, R.K.
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
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10
333-342
2005
Methanothermobacter marburgensis
brenda
Mahlert, F.; Grabarse, W.; Kahnt, J.; Thauer, R.K.; Duin, E.C.
The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states
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7
101-112
2002
Methanothermobacter marburgensis
brenda
Mahlert, F.; Bauer, C.; Jaun, B.; Thauer, R.K.; Duin, E.C.
The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2
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7
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2002
Methanothermobacter marburgensis
brenda
Duin, E.C.; Signor, L.; Piskorski, R.; Mahlert, F.; Clay, M.D.; Goenrich, M.; Thauer, R.K.; Jaun, B.; Johnson, M.K.
Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms
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9
563-576
2004
Methanothermobacter marburgensis
brenda
Goenrich, M.; Mahlert, F.; Duin, E.C.; Bauer, C.; Jaun, B.; Thauer, R.K.
Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues
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9
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2004
Methanothermobacter marburgensis
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Spectroscopic and computational studies of reduction of the metal versus the tetrapyrrole ring of coenzyme F430 from methyl-coenzyme M reductase
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Methanothermobacter marburgensis
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Characterization of alkyl-nickel adducts generated by reaction of methyl-coenzyme M reductase with brominated acids
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Methanothermobacter marburgensis
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Methanothermobacter thermautotrophicus
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Methanothermobacter marburgensis
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Methanothermobacter marburgensis
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Specific DNA binding of a potential transcriptional regulator, inosine 5-monophosphate dehydrogenase-related protein VII, to the promoter region of a methyl coenzyme M reductase I-encoding operon retrieved from Methanothermobacter thermautotrophicus strain DELTAH
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Methanothermobacter thermautotrophicus
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Characterization of the thioether product formed from the thiolytic cleavage of the alkyl-nickel bond in methyl-coenzyme M reductase
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47
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Methanothermobacter marburgensis
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Methanothermobacter marburgensis
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Methanothermobacter marburgensis
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A new mechanism for methane production from methyl-coenzyme M reductase as derived from density functional calculations
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Methanothermobacter marburgensis
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Methanobacteria
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Geometric and electronic structures of the Ni(I) and methyl-Ni(III) intermediates of methyl-coenzyme M reductase
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48
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Methanothermobacter marburgensis
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Methanothermobacter marburgensis
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Methanothermobacter marburgensis
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Localization of methyl-coenzyme M reductase as metabolic marker for diverse methanogenic Archaea
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Detection of organometallic and radical intermediates in the catalytic mechanism of methyl-coenzyme M reductase using the natural substrate methyl-coenzyme M and a coenzyme B substrate analogue
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49
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Methanothermobacter marburgensis, Methanothermobacter marburgensis OCM82
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Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues
Biochemistry
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Methanothermobacter marburgensis (P11558 and P11560 and P11562), Methanothermobacter marburgensis OCM82 (P11558 and P11560 and P11562)
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Methanothermobacter marburgensis
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Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically
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Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide
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Methanothermobacter thermautotrophicus, Methanosarcina thermophila, Methanothermobacter thermautotrophicus Marburg / DSM 2133, Methanosarcina thermophila TM-1
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Methanosarcina barkeri (P07962 and P07955 and P07964), Methanosarcina barkeri, Methanopyrus kandleri (Q49605 and Q49601 and Q49604), Methanopyrus kandleri, Methanopyrus kandleri DSM 6324 (Q49605 and Q49601 and Q49604), Methanosarcina barkeri DSM 804 (P07962 and P07955 and P07964)
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Methanosarcina barkeri, Methanothermobacter wolfeii, Methanothermobacter marburgensis
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Methanosarcina barkeri
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Methanothermobacter marburgensis
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uncultured bacterium, Methanococcales, Methanotrichaceae, Methanobacteriales, Methanocellales, Methanomicrobiales, Methanosarcinaceae, uncultured bacterium ANME-1, Methanocellales RC-I, uncultured bacterium ZC-I
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Candidatus Argoarchaeum ethanivorans
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Methanothermobacter marburgensis (P11558 and P11560 and P11562), Methanothermobacter marburgensis Marburg (P11558 and P11560 and P11562), Methanothermobacter marburgensis ATCC BAA-927 (P11558 and P11560 and P11562), Methanothermobacter marburgensis NBRC 100331 (P11558 and P11560 and P11562), Methanothermobacter marburgensis JCM 14651 (P11558 and P11560 and P11562), Methanothermobacter marburgensis DSM 2133 (P11558 and P11560 and P11562), Methanothermobacter marburgensis OCM 82 (P11558 and P11560 and P11562)
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Methanothermobacter marburgensis
brenda
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Euryarchaeota, Candidatus Bathyarchaeota, Candidatus Verstraetearchaeota
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Methanosarcina acetivorans (Q8THH1 AND Q8THG7 AND Q8THH0), Methanosarcina acetivorans, Methanosarcina acetivorans ATCC 35395 (Q8THH1 AND Q8THG7 AND Q8THH0), Methanosarcina acetivorans DSM 2834 (Q8THH1 AND Q8THG7 AND Q8THH0), Methanosarcina acetivorans JCM 12185 (Q8THH1 AND Q8THG7 AND Q8THH0)
brenda
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The radical mechanism of biological methane synthesis by methyl-coenzyme M reductase
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Methanothermobacter marburgensis (P11558 and P11560 and P11562)
brenda