EC Number   |
Cofactor |
Reference |
|---|
    1.7.2.1 | cytochrome |
contains cytochrome, probably of the c and a2 types |
644782 |
| 1.7.2.1 | cytochrome |
cytochrome c-552 or cytochrome c-553 from Pseudomonas denitrificans acts as acceptor |
644783 |
| 1.7.2.1 | cytochrome c |
- |
741908, 741932, 742316, 742802, 765354 |
| 1.7.2.1 | cytochrome cd1 |
cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer. Heme c, which transfers electrons from donor proteins into the active site, has two histidine ligands in the oxidized enzyme from Paracoccus pantotrophus. During reduction of this enzyme, Tyr25 dissociates from the distal side of heme d1, and one heme c ligand is replaced by methionine |
698736 |
| 1.7.2.1 | cytochrome cd1 |
cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer. Heme c, which transfers electrons from donor proteins into the active site, has two histidine ligands in the oxidized enzyme from Paracoccus pantotrophus. During reduction of this enzyme, Tyr25 dissociates from the distal side of heme d1, and one heme c ligand is replaced by methionine. Spectral analysis, overview |
698736 |
| 1.7.2.1 | cytochrome cd1 |
the c heme is located in a predominantly alpha-helical domain of the enzyme, whereas the d1 heme resides in a beta-propeller structure |
698810 |
| 1.7.2.1 | cytochrome cd1 |
the heme d1 is not in the oxoferryl (FeIVdO) state but is low-spin FeIII weakly coupled to a radical species, binding structure, overview |
698267 |
| 1.7.2.1 | heme |
characterization of the nitrosyl d1 heme complex by high-field-pulse electron papramagnetic spectroscopy spectra and derived 14N hyperfine and quadrupole interactions. Residue Y10 does not influence the NO ligand orientation in the reduced state in solution |
698274 |
| 1.7.2.1 | heme |
cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer |
698736 |
| 1.7.2.1 | heme |
heme c and heme d1, cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer |
698736 |
