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Literature summary for 2.8.4.1 extracted from

  • Harmer, J.; Finazzo, C.; Piskorski, R.; Ebner, S.; Duin, E.C.; Goenrich, M.; Thauer, R.K.; Reiher, M.; Schweiger, A.; Hinderberger, D.; Jaun, B.
    A nickel hydride complex in the active site of methyl-coenzyme M reductase: implications for the catalytic cycle (2008), J. Am. Chem. Soc., 130, 10907-10920.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
HS-CoM the unmethylated coenzyme M is a reversible competitive inhibitor Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CH3-S-CoM + HS-CoB Methanothermobacter marburgensis key step in the convertion of C1 substrates or acetate to methane thereby providing energy for the cell CoM-S-S-CoB + methane
-
?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
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isozyme MCR I
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Purification (Commentary)

Purification (Comment) Organism
active native isozyme MCR I in presence of HS-CoM Methanothermobacter marburgensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3-S-CoM + HS-CoB key step in the convertion of C1 substrates or acetate to methane thereby providing energy for the cell Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
?
CH3-S-CoM + HS-CoB the active enzyme is in the MCRred1c form, coordinated ligands of the two paramagnetic MCRred2 states, reduction and oxidation states and critical bond activation step, detailed overview Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
F-430 active in Ni(I) oxidation state, inactive in Ni(II) state, binding structure and oxidation states, hyperfine interactions of protons, detailed overview Methanothermobacter marburgensis