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Literature summary extracted from

  • Sarangi, R.; Dey, M.; Ragsdale, S.W.
    Geometric and electronic structures of the Ni(I) and methyl-Ni(III) intermediates of methyl-coenzyme M reductase (2009), Biochemistry, 48, 3146-3156.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.8.4.1 Ni2+ in the Ni-F430 cofactor, which is bound to the active site and exists in two oxidation states Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.4.1 2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate Methanothermobacter marburgensis i.e. CoM and CoB CoM-S-S-CoB + methane
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.4.1 Methanothermobacter marburgensis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.4.1 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 Methanothermobacter marburgensis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.4.1 2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate i.e. CoM and CoB Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.8.4.1 MCR
-
 Methanothermobacter marburgensis
2.8.4.1 methyl-coenzyme M reductase
-
 Methanothermobacter marburgensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.4.1 F-430 the Ni-F430 cofactor is bound to the active site and exists in two oxidation states Methanothermobacter marburgensis

General Information

EC Number General Information Comment Organism
2.8.4.1 metabolism MCR catalyzes the terminal step in the formation of biological methane from methyl-coenzyme M and coenzyme B Methanothermobacter marburgensis