EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
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 | Escherichia coli |
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 | Escherichia coli |
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 | Escherichia coli |
1.7.5.1 | C26A | mutant retains significant nitrate reductase activity. Mutation likely eliminates the lowest potential [4Fe-4S] cluster (center 4) | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.7.5.1 | Fe | complete coordination of the four Fe-S centers of the beta-subunit from Escherichia coli nitrate reductase | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.7.5.1 | Escherichia coli | P11349 and P09152 and P11350 | narH: P11349, narG: P09152, narI: P11350 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.7.5.1 | nitrate + reduced benzyl viologen | - |
Escherichia coli | nitrite + oxidized benzyl viologen + H2O | - |
? | |
1.7.5.1 | nitrate + tetramethyl-p-benzoquinol | i.e. duroquinol | Escherichia coli | nitrite + tetramethyl-p-benzoquinone + H2O | - |
? |