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Literature summary for 2.8.4.1 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
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Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Synonyms

Synonyms Comment Organism
MCR
-
 Methanothermobacter marburgensis
methyl-coenzyme M reductase
-
 Methanothermobacter marburgensis

Cofactor

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

General Information

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