The Enzyme Database

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EC 1.7.2.9     
Accepted name: hydroxylamine oxidase
Reaction: hydroxylamine + 3 ferricytochrome c = nitric oxide + 3 ferrocytochrome c + 3 H+
Other name(s): HOX
Systematic name: hydroxylamine:ferricytochrome-c oxidoreductase (nitric acid-forming)
Comments: The enzyme, characterized from the anaerobic ammonium-oxidizing (anammox) bacterium Kuenenia stuttgartiensis, is very similar to EC 1.7.2.6, hydroxylamine dehydrogenase. Both enzymes are homotrimeric enzymes in which each subunit contains seven c-type hemes and one specialized P460-type heme that is bound to a tyrosine residue in an adjacent subunit. However, this enzyme catalyses only the 3 electron oxidation of hydroxylamine, forming nitric oxide, and is not capable of performing further oxidation to form nitrite.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-43-8
References:
1.  Maalcke, W.J., Dietl, A., Marritt, S.J., Butt, J.N., Jetten, M.S., Keltjens, J.T., Barends, T.R. and Kartal, B. Structural basis of biological NO generation by octaheme oxidoreductases. J. Biol. Chem. 289 (2014) 1228–1242. [DOI] [PMID: 24302732]
[EC 1.7.2.9 created 2021]
 
 


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