EC Number   |
Metals/Ions |
Reference |
|---|
    2.8.4.1 | Mg2+ |
- |
393259 |
| 2.8.4.1 | Ni |
contains the nickel-containing porphinoid cofactor F-430 |
662468 |
| 2.8.4.1 | Ni |
enzyme contains the tightly-bound nickel porphinol F-430 as prosthetic group |
662466 |
| 2.8.4.1 | 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 |
662467 |
| 2.8.4.1 | Ni |
the niuckel porphinoid F-430 must be in the Ni(I) oxidation state for the enzyme to be active. The active enzyme exhibits an axial Ni(I)-based electron paramagnetic resonance signal and a UV-vis spectrum with an absorption maximum at 385 nM. This state is called the MCR-red1 state. When the temperature is lowered below 20°C the perecentage of MCR in the red2 state decreases and that in the red1 state increases. These changes with temperature are fully reversible. At most 50% of the enzyme is converted to the MCR-red2 state under all experimental conditions |
662465 |
| 2.8.4.1 | Ni(2+) |
- |
393245, 393246, 393247, 393249, 393253, 393256 |
| 2.8.4.1 | Ni(2+) |
2 mol Ni/mol enzyme |
393248 |
| 2.8.4.1 | Ni(2+) |
involved in catalytic mechanism |
393250 |
| 2.8.4.1 | Ni(2+) |
nickel-porphinoid-containing protein |
393255 |
| 2.8.4.1 | Ni(2+) |
not detected |
393257 |
