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pubmed-article:11432746pubmed:dateCreated2001-7-2lld:pubmed
pubmed-article:11432746pubmed:abstractTextMicroperoxidase 8 (MP8) is a heme octapeptide obtained by hydrolytic digestion of horse heart cytochrome c. At pH below 9, the heme iron is axially coordinated to the imidazole side chain of His18 and to a water molecule. Replacement of this weak ligand by H2O2 allows the formation of high-valent iron-oxo species which are responsible for both peroxidase-like and cytochrome P450-like activities of MP8. This paper shows that MP8 is able to catalyze the nitration of phenol by nitrite. The reaction requires H2O2 and is inhibited by ligands having a high affinity for the iron, catalase and radical scavengers. This suggests that the nitrating species could be NO2* radicals formed by the oxidation of nitrite by high-valent iron-oxo species. This new activity of MP8 opens a new access to nitro-aromatic compounds under mild conditions and validates the use of this minienzyme to mimick heme peroxidases, especially in the reactions of NO-derived species with biomolecules under oxidative stress conditions.lld:pubmed
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pubmed-article:11432746pubmed:authorpubmed-author:MansuyDDlld:pubmed
pubmed-article:11432746pubmed:authorpubmed-author:BoucherJ LJLlld:pubmed
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pubmed-article:11432746pubmed:dateRevised2007-7-23lld:pubmed
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pubmed-article:11432746pubmed:year2001lld:pubmed
pubmed-article:11432746pubmed:articleTitleMicroperoxidase 8 catalyzed nitration of phenol by nitrogen dioxide radicals.lld:pubmed
pubmed-article:11432746pubmed:affiliationLaboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, UMR 8601 CNRS, Université Paris V, France.lld:pubmed
pubmed-article:11432746pubmed:publicationTypeJournal Articlelld:pubmed
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