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Literature summary for 2.8.4.1 extracted from

  • Hinderberger, D.; Ebner, S.; Mayr, S.; Jaun, B.; Reiher, M.; Goenrich, M.; Thauer, R.K.; Harmer, J.
    Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase (2008), J. Biol. Inorg. Chem., 13, 1275-1289.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CH3-S-CoM + HS-CoB Methanothermobacter marburgensis
-
 CoM-S-S-CoB + methane
-
 ?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
 strain DSM 2133, gene mcrA
-

Purification (Commentary)

Purification (Comment) Organism
active native enzyme to homogeneity Methanothermobacter marburgensis

Reaction

Reaction Comment Organism Reaction ID
methyl-CoM + CoB = CoM-S-S-CoB + methane reaction mechanism, different varaints, the Ni(I) center is assumed to attack the thioether sulfur of CH3-S-CoM, generating -CH3 and the thiolate complex CoM-S–Ni(II)F430 as intermediates, detailed overview Methanothermobacter marburgensis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3-S-CoM + HS-CoB
-
 Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
CH3-S-CoM + HS-CoB i.e. methyl-coenzyme M + coenzyme B Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
F-430 with Ni(I) oxidation state Methanothermobacter marburgensis