The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: hydroxylamine dehydrogenase
Reaction: hydroxylamine + H2O + 4 ferricytochrome c = nitrite + 4 ferrocytochrome c + 5 H+
Other name(s): HAO (ambiguous); hydroxylamine oxidoreductase (ambiguous); hydroxylamine oxidase (misleading)
Systematic name: hydroxylamine:ferricytochrome-c oxidoreductase (nitrite-forming)
Comments: The enzymes from the nitrifying bacterium Nitrosomonas europaea [1,4] and the methylotrophic bacterium Methylococcus capsulatus [5] are hemoproteins with seven c-type hemes and one specialized P-460-type heme per subunit. The enzyme converts hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate [3]. While nitrite is the main product, the enzyme from Nitrosomonas europaea can also produce nitric oxide by catalysing the activity of EC, hydroxylamine oxidase [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-43-8
1.  Rees, M. Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I. Purification of hydroxylamine oxidase. Biochemistry 7 (1968) 353–366. [PMID: 5758552]
2.  Hooper, A.B. and Terry, K.R. Hydroxylamine oxidoreductase of Nitrosomonas. Production of nitric oxide from hydroxylamine. Biochim. Biophys. Acta 571 (1979) 12–20. [DOI] [PMID: 497235]
3.  Hooper, A.B. and Balny, C. Reaction of oxygen with hydroxylamine oxidoreductase of Nitrosomonas: fast kinetics. FEBS Lett. 144 (1982) 299–303. [DOI] [PMID: 7117545]
4.  Lipscomb, J.D. and Hooper, A.B. Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy. Biochemistry 21 (1982) 3965–3972. [PMID: 6289867]
5.  Poret-Peterson, A.T., Graham, J.E., Gulledge, J. and Klotz, M.G. Transcription of nitrification genes by the methane-oxidizing bacterium, Methylococcus capsulatus strain Bath. ISME J. 2 (2008) 1213–1220. [DOI] [PMID: 18650926]
[EC created 1972 as EC, part transferred 2012 to EC, modifed 2021, modified 2021]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald