EC Number   |
Reaction |
Reference |
|---|
   1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O |
- |
- |
| 1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O |
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket |
-, 742319 |
| 1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O |
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket |
-, 741478, 742319 |
| 1.9.6.1 | 2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O |
sulfur-shift mechanism catalytic mechanism. The second sphere type of mechanism is supported by the recent X-ray structures of Nap from Desulfovibrio desulf uricans ATCC 27774 and Cupriavidus necator H16, in which the sixth sulfur ligand of the Mo interacts with the sulfur from the cysteine residue and generates a bidentate persulfido ligand that sterically blocks the access of the substrate to the Mo ion, modelling |
742648 |
