EC 220.127.116.11 - Hydroxylamine oxidase (cytochrome)
IntEnz Enzyme Nomenclature
hydroxylamine oxidoreductase [ambiguous]
hydroxylamine oxidase [misleading]
19969 [IUBMB]hydroxylaminehydroxylamineName origin: UniProt - CHECKED (C)Formula: H3NO
Charge: 0ChEBI compound status: CHECKED (C)O2O2Name origin: UniProt - CHECKED (C)Formula: O2
Charge: 0ChEBI compound status: CHECKED (C)=H+H(+)Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)H2OH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)
The enzyme from the heterotrophic nitrifying bacterium Paracoccus denitrificans contains three to five non-heme, non-iron-sulfur iron atoms and interacts with cytochrome c556 and pseudoazurin [2,3]. Under anaerobic conditions in vitro only nitrous oxide is formed . Presumably nitroxyl is released and combines with a second nitroxyl to give nitrous oxide and water. When oxygen is present, nitrite is formed.
Links to other databases
A hydroxylamine - cytochrome C reductase occurs in the heterotrophic nitrifier Arthrobacter globiformis.Plant Cell Physiol. 26: 1439-1442 (1985).
Purification of hydroxylamine oxidase from Thiosphaera pantotropha. Identification of electron acceptors that couple heterotrophic nitrification to aerobic denitrification.FEBS Lett. 335: 246-250 (1993). [PMID: 8253206]
The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17.Biochem. J. 319: 823-827 (1996). [PMID: 8920986]
Hydroxylamine oxidation in heterotrophic nitrate-reducing soil bacteria and purification of a hydroxylamine-cytochrome c oxidoreductase from a Pseudomonas species.Arch. Microbiol. 166: 421-424 (1996). [PMID: 9082922]
[EC 18.104.22.168 created 1972 as EC 22.214.171.124, part transferred 2013 to EC 126.96.36.199, modified 2015]