Protein Variants | Comment | Organism |
---|---|---|
additional information | mutant enzyme lacking the highest-potential [4Fe-4S] cluster is devoid of menadione activity, but still retains duroquinone activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrate + 2-methyl-1,4-naphthoquinol | i.e. menadiol. As the reduction of nitrate to nitrite requires two electrons, there must necessarily be two successive bindings of quinone, with transfer of one electron to the hemes, then to the [Fe-S] cluster, to be finally accumulated at the level of the molybdenum cofactor to be able to undertake the catalytic reaction. There are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. A two-pathway electron transfer model for nitrate reductase A is proposed | Escherichia coli | nitrite + 2-methyl-1,4-naphthoquinone + H2O | - |
? | |
nitrate + tetramethyl-p-benzoquinol | i.e. duroquinol. As the reduction of nitrate to nitrite requires two electrons, there must necessarily be two successive bindings of quinone, with transfer of one electron to the hemes, then to the [Fe-S] cluster, to be finally accumulated at the level of the molybdenum cofactor to be able to undertake the catalytic reaction. There are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. A two-pathway electron transfer model for nitrate reductase A is proposed | Escherichia coli | nitrite + tetramethyl-p-benzoquinone + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
nitrate reductase A | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome | the spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete | Escherichia coli | |
heme | the spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete | Escherichia coli |