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Literature summary for 2.8.4.1 extracted from
- The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2 (2002), J. Biol. Inorg. Chem., 7, 500-513.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ni | the active purified enzyme exhibits the axial EPR signal MCR-red1 and in the presence of coenzyme M and coenzyme B the rhombic signal MCR-red2, both derived from Ni(I). Two other EPR-detectable states of the enzyme, observed in vivo and in vitro designated MCR-ox1 and MCR-ox2 have quite different nickel EPR signals and are inactive. In vitro the MCR-red2 state is converted into the MCR-ox1 state by the addition of polysulfide and into a light-sensitive MCR-ox2 state by the addition of sulfite. In the presence of O2 the MCR-red2 state is converted into a novel third state designated MCR-ox3 and exhibits two EPR signals similar but not identical to MCR-ox1 and MCR-ox2 | Methanothermobacter marburgensis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanothermobacter marburgensis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanothermobacter marburgensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MCR | - |
Methanothermobacter marburgensis |
| methyl-coenzyme M reductase | - |
Methanothermobacter marburgensis |
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