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Literature summary for 1.7.5.1 extracted from
- The coordination and function of the redox centres of the membrane-bound nitrate reductases (2001), Cell. Mol. Life Sci., 58, 179-193.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Escherichia coli | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe | coordination model for the four [Fe-S] centres of the electron-transfer subunit NarH, coordination scheme of the [Fe-S] clusters, functional role of [Fe-S] centres | Escherichia coli |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nitrate + quinol | Escherichia coli | in order to use nitrate as an electron acceptor, Escherichia coli synthesises three distinct enzymes: a membrane-bound enzyme (nitrate reductase A, NarGHI) encoded by the narGHJI operon and a soluble periplasmic nitrate reductase (NapAB, EC 1.9.6.1) encoded by the napFDAGHBC operon. A second membrane-bound nitrate reductase (nitrate reductase Z, NarZYV) encoded by the NarZYWV operon is biochemically similar to NarGHI. Whereas NarGHI synthesis is induced by nitrate under anaerobic conditions, NarZYV is expressed at a cryptic level and may assist Escherichia coli in transition from aerobic to anaerobic respiration (physiological role of this isoenzyme at the onset of the stationary growth phase in rich media). NapAB is mainly expressed in the presence of low concentrations of nitrate under both aerobic and anaerobic conditions, and its expression is suppressed at high nitrate concentrations. Conversely, NarGHI is maximally expressed when nitrate concentration is elevated, and under these conditions becomes the predominant enzyme in Escherichia coli. Thus, NapAB (Ec 1.9.6.1) and NarGHI seem to function in different ranges of nitrate concentration in a complementary way to support anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate | nitrite + quinone + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nitrate + 2-methyl-1,4-naphthoquinol | i.e. menadiol | Escherichia coli | nitrite + 2-methyl-1,4-naphthoquinone + H2O | - |
? | |
| nitrate + quinol | in order to use nitrate as an electron acceptor, Escherichia coli synthesises three distinct enzymes: a membrane-bound enzyme (nitrate reductase A, NarGHI) encoded by the narGHJI operon and a soluble periplasmic nitrate reductase (NapAB, EC 1.9.6.1) encoded by the napFDAGHBC operon. A second membrane-bound nitrate reductase (nitrate reductase Z, NarZYV) encoded by the NarZYWV operon is biochemically similar to NarGHI. Whereas NarGHI synthesis is induced by nitrate under anaerobic conditions, NarZYV is expressed at a cryptic level and may assist Escherichia coli in transition from aerobic to anaerobic respiration (physiological role of this isoenzyme at the onset of the stationary growth phase in rich media). NapAB is mainly expressed in the presence of low concentrations of nitrate under both aerobic and anaerobic conditions, and its expression is suppressed at high nitrate concentrations. Conversely, NarGHI is maximally expressed when nitrate concentration is elevated, and under these conditions becomes the predominant enzyme in Escherichia coli. Thus, NapAB (Ec 1.9.6.1) and NarGHI seem to function in different ranges of nitrate concentration in a complementary way to support anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate | Escherichia coli | nitrite + quinone + H2O | - |
? | |
| nitrate + ubiquinol | - |
Escherichia coli | nitrite + ubiquinone + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NarGHI | - |
Escherichia coli |
| NarZ | - |
Escherichia coli |
| nitrate reductase A | - |
Escherichia coli |
| nitrate reductase Z | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| bis(molybdopterin guanine dinucleotide)molybdenum cofactor | the molybdo-bis(molybdopterin guanine dinucleotide)-binding subunit NarG is organized in four domains around the molybdo-bis(molybdopterin guanine dinucleotide) cofactor | Escherichia coli | |
| heme b | the anchor subunit NarI contains two b-type hemes. Electron transfer out of NarI is mediated by two hemes, one of relatively low midpoint potential Em (heme bL), and one of relatively high Em (heme bH) | Escherichia coli | |
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