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Biochim Biophys Acta. 1999 May 5;1411(2-3):290-309.

Nitric oxide and iron proteins.

Author information

1
Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK. ccooper@essex.ac.uk

Abstract

Nitric oxide interactions with iron are the most important biological reactions in which NO participates. Reversible binding to ferrous haem iron is responsible for the observed activation of guanylate cyclase and inhibition of cytochrome oxidase. Unlike carbon monoxide or oxygen, NO can also bind reversibly to ferric iron. The latter reaction is responsible for the inhibition of catalase by NO. NO reacts with the oxygen adduct of ferrous haem proteins (e.g. oxyhaemoglobin) to generate nitrate and ferric haem; this reaction is responsible for the majority of NO metabolism in the vasculature. NO can also interact with iron-sulphur enzymes (e.g. aconitase, NADH dehydrogenase). This review describes the underlying kinetics, thermodynamics, mechanisms and biological role of the interactions of NO with iron species (protein and non-protein bound). The possible significance of iron reactions with reactive NO metabolites, in particular peroxynitrite and nitroxyl anion, is also discussed.

PMID:
10320664
DOI:
10.1016/s0005-2728(99)00021-3
[Indexed for MEDLINE]
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