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Literature summary for 2.8.4.1 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

Metals/Ions Comment Organism Structure
Ni2+ nickel center in the ox1 form of methylcoenzyme M reductase, MCRox1 Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
MCRox1
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Methanothermobacter marburgensis
methylcoenzyme M reductase
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Methanothermobacter marburgensis

Cofactor

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