Nitroxyl oxidizes NADPH in a superoxide dismutase inhibitable manner
Nitroxyl oxidizes NADPH in a superoxide dismutase inhibitable manner
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.
NO synthase, nitroxyl, NADPH, superoxide dismutase, nitrite, nitrate, peroxynitrite, free radicals
803-8
Reif, Andreas
ed3a7ef3-c323-4416-8df2-dd09bfcc456c
Zecca, Luigi
7f91a099-5aa7-42b0-a7f3-9daec65a8913
Riederer, Peter
265a1573-aeac-4736-ade4-4082032d97d1
Feelisch, Martin
8c1b9965-8614-4e85-b2c6-458a2e17eafd
Schmidt, Harald H.H.W.
28ef9449-82f1-4e55-b92c-7ed73f714513
1 April 2001
Reif, Andreas
ed3a7ef3-c323-4416-8df2-dd09bfcc456c
Zecca, Luigi
7f91a099-5aa7-42b0-a7f3-9daec65a8913
Riederer, Peter
265a1573-aeac-4736-ade4-4082032d97d1
Feelisch, Martin
8c1b9965-8614-4e85-b2c6-458a2e17eafd
Schmidt, Harald H.H.W.
28ef9449-82f1-4e55-b92c-7ed73f714513
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), .
(doi:10.1016/S0891-5849(01)00477-4).
(PMID:11275480)
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.
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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
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Date deposited: 22 Jun 2012 14:10
Last modified: 15 Mar 2024 03:41
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Contributors
Author:
Andreas Reif
Author:
Luigi Zecca
Author:
Peter Riederer
Author:
Harald H.H.W. Schmidt
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