EC Number   |
Cofactor |
Reference |
|---|
   1.7.2.2 | cytochrome c |
an enzyme-bound c-type cytochrome with a non-canonical CX2CK motif. CcmI, i.e. cytochrome c maturation system I, an apocytochrome c chaperone, is important and essential for maturation of c-type cytochromes with the non-canonical heme binding motif (HBM) CX2CK, presumably by ensuring that heme attachment at canonical HBMs occurs before apoprotein degradation. Both CcmISo-1 and CcmISo-2 are required for maturation of NrfA. The periplasmic portion of CcmI, CcmI-2, interacts with C-terminus of enzyme NrfA. Heme attachment to the apoprotein is achieved stereochemically by linking of the 2-vinyl and 4-vinyl of heme b via thioether bonds to the N-terminal and C-terminal cysteines, respectively, within heme binding motif. NrfASo is unstable unless heme attachment is timely accomplished, the failure of heme ligation in NrfASo results in rapid degradation, NrfA is rapidly degraded unless properly maturated |
743309 |
| 1.7.2.2 | cytochrome c |
heme |
742740 |
| 1.7.2.2 | cytochrome c |
multiheme |
743303 |
| 1.7.2.2 | Ferredoxin |
[4Fe-4S]-ferredoxin cofactor |
696159 |
| 1.7.2.2 | heme |
- |
671934, 696256, 698876, 711343 |
| 1.7.2.2 | heme |
10 heme centres range in reduction potential from -30 to 320 mV. The heme oxidation state has a profound effect on the interactions with substrate molecules, nitrite and hydroxylamine |
658229 |
| 1.7.2.2 | heme |
7.5 units heme per subunit |
672400 |
| 1.7.2.2 | heme |
a multiheme enzyme |
712510 |
| 1.7.2.2 | heme |
an octaheme cytochrome c nitrite reductase |
710714 |
| 1.7.2.2 | heme |
catalytic heme in the Fe2+ state |
742740 |
