EC Number   |
Cofactor |
Reference |
|---|
   1.8.2.2 | cytochrome c |
- |
676077, 741526, 763985, 764941, 765056, 765356 |
| 1.8.2.2 | cytochrome c |
a diheme c-type cytochrome. The enzyme contains two typical class I c-type cytochrome domains wrapped around two hemes axially coordinated by His53/Cys96 and His164/Lys208. These domains are very similar, suggesting a gene duplication event during evolution. A ligand switch from Lys208 to Met209 is observed upon reduction of the enzyme. Heme 2 is the electron exit point |
742887 |
| 1.8.2.2 | cytochrome c |
diheme cytochrome c TsdA, Allochromatium vinosum does not contain a second diheme cytochrome TsdB. Structure modelling, overview |
742899 |
| 1.8.2.2 | cytochrome c |
diheme cytochrome c TsdB acts as an effective electron acceptor of TsdA in vitro when TsdA and TsdB originate from the same source organism. TsdAB tetraheme cytochrome c in the oxidized state contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Thiosulfate is covalently bound to Cys330 on heme 3. TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism. The four hemes are covalently bound to the polypeptide chain through thioether bonds formed by cysteine residues Cys21 and Cys24 for heme 1, Cys121 and Cys124 for heme 2, Cys287and Cys290 for heme 3, and Cys402 and Cys405 for heme 4, three hemes (hemes 1, 2, and 4) with His/Met coordination. Heme 3 exhibits axial ligation by His291, and the Sgamma atom of Cys330 is located in close vicinity to the heme iron such that it serves as the sixth ligand. Heme structure modelling, overview |
742899 |
| 1.8.2.2 | cytochrome c3 |
- |
740640 |
| 1.8.2.2 | Ferricytochrome |
- |
673503 |
| 1.8.2.2 | heme |
- |
765056 |
| 1.8.2.2 | heme |
diheme cytochrome c, residues methionine M222 or M236 and cysteine C123 are probable sixth distal axial ligands of the two heme irons |
724861 |
| 1.8.2.2 | heme |
ferric heme, the enzyme shows unusual histidine-cysteine axial heme coordination. Heme structure analysis, detailed overview |
742887 |
| 1.8.2.2 | heme |
reduction of His/Cys-ligated heme 1 occurs reversibly between approximately -100 and -350 mV. Reduction of His/Lys-ligated heme 2 is proposed to occur between approximately +150 and -100 mV |
740755 |
