EC Number   |
Cofactor |
Reference |
|---|
   1.11.1.5 | cytochrome c |
holo CcP binds cytochrome c with micromolar affinity. For apo CcP, the interaction with cytochrome c is completely abolished |
741899 |
| 1.11.1.5 | cytochrome c |
study on both chemical shift perturbations and paramagnetic relaxation enhancements effects in the NMR spectrum of CcP generated in the presence of spin-labelled cytochrome c |
742511 |
| 1.11.1.5 | cytochrome c |
thermodynamic affinity constants for binding the first and second cytochrome c are KI 0.0000001 per M, KII 0.0001 per M. Cytochrome c binds at the weaker-binding site with relatively great affinity, and places upper bounds on the contributions of repulsion between the two cytochrome c of the ternary complex |
741907 |
| 1.11.1.5 | heme |
- |
711231, 724337, 724372, 724463, 724658, 726385 |
| 1.11.1.5 | heme |
diheme cytochrome c peroxidase |
724008, 724366 |
| 1.11.1.5 | heme |
diheme enzyme |
764157 |
| 1.11.1.5 | heme |
diheme enzyme. L-heme is five-coordinate (5C) and (presumably) high-spin. H-heme is required for the L-heme to become 5C (no water or exogenous ligand bound) |
764157 |
| 1.11.1.5 | heme |
Fe(III) reduction to Fe(IV) in heme cofactor, pH dependence of the reduction potential and heme binding site structure analysis of wild-type and mutant enzymes using photoreduction and spectroscopic methods, respectively, overview |
725645 |
| 1.11.1.5 | heme |
heme-associated peroxidase activity |
687074 |
| 1.11.1.5 | heme |
the enzyme bears three heme c-binding motifs |
725756 |
