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Literature summary extracted from

  • Kern, D.I.; Goenrich, M.; Jaun, B.; Thauer, R.K.; Harmer, J.; Hinderberger, D.
    Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy (2007), J. Biol. Inorg. Chem., 12, 1097-1105.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.8.4.1 Ni2+ each active site has the nickel porphyrinoid F430 as a prosthetic group, in the active state, F430 contains the transition metal in the Ni(I) oxidation state 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 CH3-S-CoM + HS-CoB Methanothermobacter marburgensis i.e. methyl-coenzyme M + coenzyme B CoM-S-S-CoB + methane
-
 ?
2.8.4.1 additional information Methanothermobacter marburgensis the enzyme catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.4.1 Methanothermobacter marburgensis
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 i.e. Methanothermobacter thermoautotrophicum strain Marburg, DSM 2133
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2.8.4.1 Methanothermobacter marburgensis
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 or Methanothermobacter thermoautotrophicum strain Marburg, DSM 2133
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.4.1 active native MCR Methanothermobacter marburgensis
2.8.4.1 native enzyme, during purification the enzyme lost its MCR-red2 signal owing to the removal of HS-CoB Methanothermobacter marburgensis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.8.4.1 additional information growth temperature 65°C Methanothermobacter marburgensis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.4.1 CH3-S-CoM + HS-CoB i.e. methyl-coenzyme M + coenzyme B Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
2.8.4.1 CH3-S-CoM + HS-CoB i.e. methyl-coenzyme M or 2-methylmercaptoethanesulfonate + coenzyme B or N-7-mercaptoheptanoylthreonine phosphate Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
2.8.4.1 additional information the enzyme catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea Methanothermobacter marburgensis ?
-
 ?
2.8.4.1 additional information MCR reduction/oxidation state, electron paramagnetic resonance status analysis, detailed overview Methanothermobacter marburgensis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.4.1 More enzyme structure analysis in reduced and oxidized state, the enzyme has two structurally interlinked active sites embedded in an a2b2c2 subunit structure, overview Methanothermobacter marburgensis
2.8.4.1 More the enzyme has two structurally interlinked active sites embedded in an alpha2beta2gamma2 subunit structure. Each active site has the nickel porphyrinoid F430 as a prosthetic group Methanothermobacter marburgensis

Synonyms

EC Number Synonyms Comment Organism
2.8.4.1 MCR
-
 Methanothermobacter marburgensis
2.8.4.1 methyl-coenzyme M reductase
-
 Methanothermobacter marburgensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.4.1 coenzyme F430 each active site has the nickel porphyrinoid F430 as a prosthetic group, in the active state, F430 contains the transition metal in the Ni(I) oxidation state Methanothermobacter marburgensis
2.8.4.1 F-430 the enzyme has two structurally interlinked active sites embedded in an alpha2beta2gamma2 subunit structure. Each active site has the nickel porphyrinoid F430 as a prosthetic group. In the active state, F430 contains the transition metal in the Ni(I) oxidation state Methanothermobacter marburgensis