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Literature summary for 2.8.4.1 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
Search for more literature for 2.8.4.1

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CH3-S-CoM + HS-CoB Methanothermobacter marburgensis i.e. methyl-coenzyme M + coenzyme B CoM-S-S-CoB + methane
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 ?
additional information Methanothermobacter marburgensis the enzyme catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea ?
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 ?

Organism

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

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

Source Tissue

Source Tissue Comment Organism Textmining
additional information growth temperature 65°C Methanothermobacter marburgensis
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Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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

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

Cofactor

Cofactor Comment Organism Structure
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
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