EC Number   |
Reaction |
Reference |
|---|
    1.16.3.1 | 4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O |
A multi-copper protein: ceruloplasmin from animals, rusticyanin in Thiobacillus ferroxidans |
- |
| 1.16.3.1 | 4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O |
iron binding site plays a major role in tuning the reduction potenzial of iron to provide a large driving force for the reaction, E185 residue provides the dominant electron transfer pathway to the T1 Cu site |
658983 |
| 1.16.3.1 | 4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O |
reaction mechanism, overview. Two reaction steps: 1. 2 Fe2+ O2 + 2 H+ = 2 Fe3+ + H2O2 and 2. H2O2 + 2 Fe2+ + 2 H+ = 2 Fe3+ + 2 H2O. The second step is rate-limiting |
714969 |
| 1.16.3.1 | 4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O |
residues D283, E185, D409 provide a Fe(II) binding site that favors ferric ion thus reducing the reduction potential of the bound Fe(II). Residues E185 and D409 form part of the electron-transfer pathway from the bound Fe(II) to the proteins type I Cu(II) |
672085 |
