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.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Mar 5 2004|
Bibliographical noteFunding Information:
The author (M.S.) was the recipient of an IARC postdoctoral fellowship and this study was carried out under the postdoctoral training program funded by the International Agency for Research on Cancer (WHO), Lyon, France. The authors thank Dr. J. Cheney for editing the manuscript and Mrs. P. Collard for secretarial assistance.
- Angeli's salt
- Nitric oxide
- Xanthine oxidase