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Nitroxyl oxidizes NADPH in a superoxide dismutase inhibitable manner

Record type: Article

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.

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Citation

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 & Medicine, 30, (7), pp. 803-8. (doi:10.1016/S0891-5849(01)00477-4). (PMID:11275480).

More information

e-pub ahead of print date: 21 March 2001
Published date: 1 April 2001
Keywords: NO synthase, nitroxyl, NADPH, superoxide dismutase, nitrite, nitrate, peroxynitrite, free radicals
Organisations: Clinical & Experimental Sciences

Identifiers

Local EPrints ID: 337871
URI: http://eprints.soton.ac.uk/id/eprint/337871
ISSN: 0891-5849
PURE UUID: c24e929e-9ea2-49f9-9e89-1e8fd02ca888
ORCID for Martin Feelisch: ORCID iD orcid.org/0000-0003-2320-1158

Catalogue record

Date deposited: 22 Jun 2012 14:10
Last modified: 18 Jul 2017 06:00

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Contributors

Author: Andreas Reif
Author: Luigi Zecca
Author: Peter Riederer
Author: Martin Feelisch ORCID iD
Author: Harald H.H.W. Schmidt

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