EC Number   |
Cofactor |
Reference |
|---|
    1.8.3.1 | cytochrome b5 |
- |
741618 |
| 1.8.3.1 | cytochrome b5 |
crystal structure of the cytochrome b5 domain |
657446 |
| 1.8.3.1 | cytochrome c |
- |
741495, 741618, 742912, 743226 |
| 1.8.3.1 | cytochrome c |
ferric cytochrome c, Fe3+ cyt c, cytochrome c is known to participate in mitochondrial respiration and has antioxidant and peroxidase activities. Fe3+ cyt c might have a role in the deleterious effects of sulfite in biological systems due to increased production of sulfite radical. Mammalian cytochrome c (cyt c) is a small, globular protein that exists in high concentrations in the inner membrane of mitochondria |
741809 |
| 1.8.3.1 | cytochrome c |
natural electron acceptor cytochrome c |
742364 |
| 1.8.3.1 | heme |
- |
392990, 392999, 393008, 393013, 393015, 393028, 698227, 712146, 713343, 742912, 743226, 764105, 764106, 765392, 765870 |
| 1.8.3.1 | heme |
interactions of residue H90 with a heme propionate group destabilize the Fe(III) state of the heme |
724810 |
| 1.8.3.1 | heme |
the enzyme contains a heme group per subunit |
765817 |
| 1.8.3.1 | heme |
the heme accepts electrons from the Mo ion following sulfite oxidation, a flexible connects the Mo and heme domains |
742364 |
| 1.8.3.1 | Molybdenum |
molybdoenzyme |
659599 |
