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Literature summary extracted from

  • Gonzalez, E.; Ghosh, A.
    Models of the ox1 state of methylcoenzyme M reductase: where are the electrons? (2008), Chemistry, 14, 9981-9989.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.8.4.1 Ni2+ nickel center in the ox1 form of methylcoenzyme M reductase, MCRox1 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)ethansulfonate + 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
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.8.4.1 MCRox1
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 Methanothermobacter marburgensis
2.8.4.1 methylcoenzyme M reductase
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 Methanothermobacter marburgensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.4.1 F-430 an active site Ni cofactor Methanothermobacter marburgensis