Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ni2+ | in the coenzyme F430, a redox-active nickel tetrahydrocorphin bound at the active site | Methanothermobacter marburgensis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Methanothermobacter marburgensis | the enzyme catalyzes the final step in methane biosynthesis by methanogenic archaea | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanothermobacter marburgensis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme | Methanothermobacter marburgensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme catalyzes the final step in methane biosynthesis by methanogenic archaea | Methanothermobacter marburgensis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MCR | - |
Methanothermobacter marburgensis |
methyl-coenzyme M reductase | - |
Methanothermobacter marburgensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
coenzyme F430 | a redox-active nickel tetrahydrocorphin bound at the active site, contains low-spin Ni(II), determination of the cofactor reduction site at the exocyclic ketone group by NMR study, mass spectrometry, and QM/MM computations, conversion of F430 to F330 reduces the hydrocorphin ring but not the metal, reduction of F430 with Ti(III) citrate to generate F380, corresponding to the active MCRred1 state, reduces the Ni(II) to Ni(I) but does not reduce the tetrapyrrole ring system, overview | Methanothermobacter marburgensis |