EC Number   |
Reaction |
Reference |
|---|
   1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O |
kinetics |
394634 |
| 1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O |
kinetics, energy, catalysis information |
394630, 394631 |
| 1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O |
only ferrocytochrome c bound at the Pelletier-Kraut site of enzyme is oxidized during turnover |
672215 |
| 1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O |
pseudo-first-order kinetics |
659522 |
| 1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O |
reaction scheme |
394609 |
| 1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O |
the enzyme uses hydrogen peroxide as an electron acceptor to oxidize cytochrome c. The enzyme is not essential for both cell viability and respiration. Its biological function is to reduce H2O2 generated during aerobic respiratory process. The enzyme may also act as a peroxynitrite scavenger |
658180 |
| 1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O |
the intermediate Compound I forms once H2O2 is heterolytically cleaved, releasing a water molecule. The remaining O atom oxidizes the heme iron to Fe(IV) and an organic moiety to a cation radical. For most heme peroxidases, this moiety is the porphyrin ring. Upon two electron transfer events from two substrate molecules, the enzyme returns to the resting state with water occupying the active site |
724335 |
