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Free Radic Biol Med. 2001 Apr 1;30(7):803-8.

Nitroxyl oxidizes NADPH in a superoxide dismutase inhibitable manner.

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1
Clinical Neurochemistry, Department of Psychiatry and Psychotherapy, Julius-Maximilians-University, W├╝rzburg, Germany. a.reif@gmx.net

Abstract

Nitric oxide synthases (NOS) convert L-arginine and N(omega)-hydroxy-L-arginine to nitric oxide (*NO) and/or nitroxyl (NO(-)) in a NADPH-dependent fashion. Subsequently, *NO/superoxide (O(2-)-derived peroxynitrite (ONOO(-)) consumes one additional mol NADPH. The related stoichiometry of NO(-) and NADPH is unclear. We here describe that NO(-) also oxidizes NADPH in a concentration-dependent manner. In the presence of superoxide dismutase (SOD), which also converts NO(-) to *NO, nitrite accumulation was almost doubled and no oxidation of NADPH was observed. Nitrate yield from NO(-) was low, arguing against intermediate ONOO(-) formation. Thus, biologically formed NO(-) may function as an effective pro-oxidant unless scavenged by SOD and affect the apparent NADPH stoichiometry of the NOS reaction.

PMID:
11275480
[Indexed for MEDLINE]
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