| Hydroxylamine Oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.7.3.4 | ||||||||
| CAS no. | 9075-43-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Hydroxylamine oxidoreductase (HAO) is an enzyme found in the prokaryotic genus Nitrosomonas. It plays a critically important role in the biogeochemical nitrogen cycle as part of the metabolism of ammonia-oxidizing bacteria.
The substrate is hydroxylamine (), a chemical produced biologically by the enzyme Ammonia monooxygenase. The products of the catalyzed reaction are debated, but recent work shows compelling evidence for the production of nitric oxide.[1]
- ^ Caranto, Jonathan D.; Lancaster, Kyle M. (2017-07-17). "Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase". Proceedings of the National Academy of Sciences. 114 (31): 8217–8222. Bibcode:2017PNAS..114.8217C. doi:10.1073/pnas.1704504114. ISSN 0027-8424. PMC 5547625. PMID 28716929.