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Xanthine oxidase converts nitric oxide to nitroxyl that inactivates the enzyme.

Abstract：

:Xanthine oxidase (XO) was found to convert nitric oxide (NO* ) released from spermine-NONOate to nitroxyl (HNO), the one-electron reduction product of NO*, in the presence of its substrate hypoxanthine under anaerobic conditions. Under these conditions, XO lost its activity. Upon aerobic incubation of XO with its substrate, neither conversion of NO* to HNO nor inactivation of the enzyme was observed. Angeli's salt (an HNO generator) or synthetic peroxynitrite inactivated XO at low concentrations, whereas high concentrations of diethylamine-NONOate (an NO* donor) and SIN-1 (which generates peroxynitrite by releasing both NO* and superoxide) were required to inactivate XO. These results suggest that HNO generated by XO under anaerobic conditions inactivates XO. As both XO and NO* synthase are activated and/or induced in ischemia-reperfusion injury, HNO formed by XO may contribute to pathogenesis by exerting its potent oxidation activity against a variety of biological compounds.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Saleem M,Ohshima H

doi

10.1016/j.bbrc.2004.01.081

subject

Has Abstract

pub_date

2004-03-05 00:00:00

pages

455-62

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X04001275

journal_volume

315

pub_type

杂志文章

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