Protective Effect of Dinitrosyl Iron Complexes Bound with Hemoglobin on Oxidative Modification by Peroxynitrite.

Olga V Kosmachevskaya,Alexey F Topunov,Natalia N Novikova,Elvira I Nasybullina,Konstantin B Shumaev

doi:10.3390/ijms222413649

Olga V Kosmachevskaya, Alexey F Topunov + Show 3 more

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https://doi.org/10.3390/ijms222413649

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Abstract

Dinitrosyl iron complexes (DNICs) are a physiological form of nitric oxide (•NO) in an organism. They are able not only to deposit and transport •NO, but are also to act as antioxidant and antiradical agents. However, the mechanics of hemoglobin-bound DNICs (Hb-DNICs) protecting Hb against peroxynitrite-caused, mediated oxidative modification have not yet been scrutinized. Through EPR spectroscopy we show that Hb-DNICs are destroyed under the peroxynitrite action in a dose-dependent manner. At the same time, DNICs inhibit the oxidation of tryptophan and tyrosine residues and formation of carbonyl derivatives. They also prevent the formation of covalent crosslinks between Hb subunits and degradation of a heme group. These effects can arise from the oxoferryl heme form being reduced, and they can be connected with the ability of DNICs to directly intercept peroxynitrite and free radicals, which emerge due to its homolysis. These data show that DNICs may ensure protection from myocardial ischemia.

Highlights

Dinitrosyl iron complexes (DNICs) are a physiological form of nitric oxide (NO) in an organism, depositing NO and transferring it to various biological targets [1,2,3]
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In this work we studied the effect of Hb-bound DNICs on the oxidative Hb modification caused by peroxynitrite

Summary

Introduction

Dinitrosyl iron complexes (DNICs) are a physiological form of nitric oxide (NO) in an organism, depositing NO and transferring it to various biological targets [1,2,3]. It should be noticed that as nitric oxide is a radical molecule, we indicate it as NO, very often it is written : NO

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