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Literature summary for 1.7.3.6 extracted from
- Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner (2013), Biochemistry, 52, 6211-6218 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified native enzyme, mixing of 0.002 ml of protein in 20 mM Tris-HCl, pH 8.1, with 0.002 ml of crystallization solution containing 0.1 M potassium nitrate, 0.1 M MES-Na buffer, pH 7.5, and 46% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.1 A resolution, modelling | Nitrosomonas europaea |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Nitrosomonas europaea | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hydroxylamine + 2 ferricytochrome c | Nitrosomonas europaea | - |
nitroxyl + 2 ferrocytochrome c + 2 H+ | - |
? |  |
| nitroxyl + 2 ferrocytochrome c + O2 + H+ | Nitrosomonas europaea | - |
nitrite + 2 ferricytochrome c + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Nitrosomonas europaea | Q82V11 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme by ammonium sulfate fractionation, gel filtration, ultracentrifugation, again gel filtration, followed by anion exchange chromatography | Nitrosomonas europaea |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hydroxylamine + 2 ferricytochrome c | - |
Nitrosomonas europaea | nitroxyl + 2 ferrocytochrome c + 2 H+ | - |
? | |
| nitroxyl + 2 ferrocytochrome c + O2 + H+ | - |
Nitrosomonas europaea | nitrite + 2 ferricytochrome c + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotrimer | 3 * 67000, SDS-PAGE | Nitrosomonas europaea |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HAO | - |
Nitrosomonas europaea |
| hydroxylamine oxidoreductase | - |
Nitrosomonas europaea |
| protein NE1300 | - |
Nitrosomonas europaea |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome c554 | - |
Nitrosomonas europaea | |
| cytochrome P-460 | one heme in each HAO monomer is a highly unusual heme P460 that is the site of catalysis. Heme P460 contains two covalent cross-links between the porphyrin and a Tyr residue, structure analysis, overview | Nitrosomonas europaea | |
| heme | hydroxylamine oxidoreductase is a 24-heme homotrimeric enzyme | Nitrosomonas europaea | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | one heme in each HAO monomer is a highly unusual heme P460 that is the site of catalysis, Enzyme structure analysis and molecular docking, modelling | Nitrosomonas europaea |
| physiological function | enzyme HAO catalyzes the conversion of hydroxylamine to nitrite in nitrifying bacteria, that is key reaction in the nitrogen cycle. The enzyme HAO, protein NE1300, may play a structural role in the ternary complex with cytochrome c554, the physiological electron acceptor of HAO. Two of HAO's product electrons are subsequently transferred back to ammonia monooxygenase as substrate electrons, and the other two electrons contribute to the electrochemical gradient through a terminal oxidase in the cytoplasmic membrane | Nitrosomonas europaea |
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