EC Number   |
Reaction |
Reference |
|---|
    1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
a copper protein, cytochrome c-552 or cytochrome c-553 from Pseudomonas denitrificans acts as acceptor |
644783 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
catalytic mechansim, overview |
-, 742316 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
electron transfer from c heme to d1 heme is very slow, order of seconds |
395073 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
electron-transfer mechanism |
395067 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
mechanism |
644787 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
ordered mechanism in which electron transfer is gated by binding of nitrite to the type 2 Cu centre |
699530 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
proposed reaction mechanism |
395063 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
rate constants of intermolecular electron transfer |
395075 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
reaction mechanism, overview. Mobility of two residues essential to catalytic activity, Asp98 and His244, are sterically restricted in GtNIR by Phe109 on a characteristic loop structure that is found above Asp98 and by an unusually short CH-O hydrogen bond observed between His244 and water, respectively. Analysis of the hydrogen-bond networks around His244 and the flow path of protons consumed by nitrite reduction. The electron transfer reaction is coupled with the proton transfer reaction |
-, 742802 |
| 1.7.2.1 | nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ |
reaction mechanism, overview. The transformation from the initial O-coordination of substrate to the final N-coordination of product is achieved by electron transfer from T1 copper to T2 copper, rather than by the previously reported side-on coordination of a NO intermediate, which only takes place in the reduced enzyme. Role of structural change in the critical residue Asp98, which affects the energetics of substrate attachment and product release at the T2 copper reaction center, while it does not significantly affect the activation energy and reaction pathways of the nitrite reduction process |
741908 |
