EC Number   |
Protein Variants |
Reference |
|---|
   1.7.5.1 | C196A |
mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme |
696187 |
| 1.7.5.1 | C227A |
mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme |
696187 |
| 1.7.5.1 | C263A |
mutant retains significant nitrate reductase activity. EPR analysis shows that the highest redox potential [4Fe-4S] cluster (center 1) is selectively removed by the C263A mutation |
696187 |
| 1.7.5.1 | C26A |
mutant retains significant nitrate reductase activity. Mutation likely eliminates the lowest potential [4Fe-4S] cluster (center 4) |
696187 |
| 1.7.5.1 | G65A |
site-directed mutageness of subunit NarI, mutant G65A is able to support growth and retains significant quinol:nitrate oxidoreductase activity |
741900 |
| 1.7.5.1 | H187Y |
mutant lacking heme bL but having heme bH, the heme reduction by menadiol is abolished |
696200 |
| 1.7.5.1 | H187Y |
mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed |
696212 |
| 1.7.5.1 | H187Y |
mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed |
696212 |
| 1.7.5.1 | H205Y |
mutant without heme bH but with heme bL, a smaller and slower heme reduction compared to that of the wild-type enzyme is observed. A transient species, likely to be associated with a semiquinone radical anion, is generated not only on reduction of the wild-type enzyme but also on reduction of NarGHIH56R and NarGHIH205Y. Compared to the wild type, no significant heme reoxidation is observed for NarGHIH56R and NarGHIH205Y. This result indicates that a single mutation removing heme bH blocks the electron-transfer pathway from the subunit NarI to the catalytic dimer NarGH |
696200 |
| 1.7.5.1 | H49C |
the mutant lacks catalytic activity |
-, 712493 |
