Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Escherichia coli K-12 | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrate + ferrocytochrome | Escherichia coli K-12 | NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC | nitrite + ferricytochrome + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli K-12 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrate + ferrocytochrome | NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC | Escherichia coli K-12 | nitrite + ferricytochrome + H2O | - |
? | |
nitrate + ferrocytochrome | the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB | Escherichia coli K-12 | nitrite + ferricytochrome + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the nap operon of Escherichia coli K-12, encoding a periplasmic nitrate reductase, encodes seven proteins. The catalytic complex in the periplasm, NapANapB receives electrons from the quinol pool via the membrane-bound cytochrome NapC. Like NapA, B and C, NapD, is also essential for Nap activity. None of the remaining three polypeptides, NapF, G and H, which are predicted to encode non-heme, iron-sulfur proteins, are essential for Nap activity | Escherichia coli K-12 |
Synonyms | Comment | Organism |
---|---|---|
periplasmic nitrate reductase | - |
Escherichia coli K-12 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome | the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB | Escherichia coli K-12 |