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Reif, A. et al.

Reif, Zecca, Riederer, Feelisch, Schmidt,

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.[1]

References

Nitroxyl oxidizes NADPH in a superoxide dismutase inhibitable manner. Reif, A., Zecca, L., Riederer, P., Feelisch, M., Schmidt, H.H. Free Radic. Biol. Med. (2001) [Pubmed]

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