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• W2080470337 endingPage "6329" @default.
• W2080470337 startingPage "6317" @default.
• W2080470337 abstract "Oxygenated heme proteins are known to react rapidly with nitric oxide (NO) to produce peroxynitrite (PN) at the heme site. This process could lead either to attenuation of the effects of NO or to nitrosative protein damage. PN is a powerful nitrating and oxidizing agent that has been implicated in a variety of cell injuries. Accordingly, it is important to delineate the nature and variety of reaction mechanisms of PN interactions with heme proteins. In this Forum, we survey the range of reactions of PN with heme proteins, with particular attention to myoglobin and cytochrome c. While these two proteins are textbook paradigms for oxygen binding and electron transfer, respectively, both have recently been shown to have other important functions that involve NO and PN. We have recently described direct evidence that ferrylmyolgobin (ferrylMb) and nitrogen dioxide (NO2) are both produced during the reaction of PN and metmyolgobin (metMb) (Su, J.; Groves, J. T. J. Am. Chem. Soc. 2009, 131, 12979−12988). Kinetic evidence indicates that these products evolve from the initial formation of a caged radical intermediate [FeIV═O·NO2]. This caged pair reacts mainly via internal return with a rate constant kr to form metMb and nitrate in an oxygen-rebound scenario. Detectable amounts of ferrylMb are observed by stopped-flow spectrophotometry, appearing at a rate consistent with the rate, kobs, of heme-mediated PN decomposition. Freely diffusing NO2, which is liberated concomitantly from the radical pair (ke), preferentially nitrates myoglobin Tyr103 and added fluorescein. For cytochrome c, Raman spectroscopy has revealed that a substantial fraction of cytochrome c converts to a β-sheet structure, at the expense of turns and helices at low pH (Balakrishnan, G.; Hu, Y.; Oyerinde, O. F.; Su, J.; Groves, J. T.; Spiro, T. G. J. Am. Chem. Soc., 2007, 129, 504−505). It is proposed that a short β-sheet segment, comprising residues 37−39 and 58−61, extends itself into the large 37−61 loop when the latter is destabilized by protonation of H26, which forms an anchoring hydrogen bond to loop residue P44. This conformation change ruptures the Met80−Fe bond, as revealed by changes in ligation-sensitive Raman bands. It also induces peroxidase activity with the same temperature profile. This process is suggested to model the apoptotic peroxidation of cardiolipin by cytochrome c." @default.
• W2080470337 created "2016-06-24" @default.
• W2080470337 creator A5051900499 @default.
• W2080470337 creator A5071583821 @default.
• W2080470337 date "2010-07-12" @default.
• W2080470337 modified "2023-10-16" @default.
• W2080470337 title "Mechanisms of Peroxynitrite Interactions with Heme Proteins" @default.
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