Nitroxyl oxidizes NADPH in a superoxide dismutase inhibitable manner


Reif, Andreas, Zecca, Luigi, Riederer, Peter, Feelisch, Martin and Schmidt, Harald H.H.W. (2001) Nitroxyl oxidizes NADPH in a superoxide dismutase inhibitable manner. Free Radical Biology and Medicine, 30, (7), 803-8. (doi:10.1016/S0891-5849(01)00477-4). (PMID:11275480).

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Description/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.

Item Type: Article
ISSNs: 0891-5849 (print)
Keywords: NO synthase, nitroxyl, NADPH, superoxide dismutase, nitrite, nitrate, peroxynitrite, free radicals
Subjects: Q Science > QP Physiology
Q Science > QR Microbiology > QR180 Immunology
Divisions: Faculty of Medicine > Infection, Inflammation and Immunity
ePrint ID: 337871
Date Deposited: 22 Jun 2012 14:10
Last Modified: 27 Mar 2014 20:21
URI: http://eprints.soton.ac.uk/id/eprint/337871

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