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血红蛋白结合的二硝酰基铁复合物对过氧亚硝酸酯氧化修饰的保护作用。

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

机构信息

Research Center of Biotechnology of the Russian Academy of Sciences, Bach Institute of Biochemistry, 119071 Moscow, Russia.

National Research Center, Kurchatov Institute, 123182 Moscow, Russia.

出版信息

Int J Mol Sci. 2021 Dec 20;22(24):13649. doi: 10.3390/ijms222413649.

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.

摘要

二硝酰基铁复合物(DNICs)是生物体内一氧化氮(NO)的一种生理形式。它们不仅能够储存和运输 NO,还可以作为抗氧化剂和抗自由基剂。然而,血红蛋白结合的二硝酰基铁复合物(Hb-DNICs)保护血红蛋白免受过氧亚硝酸盐引起的介导的氧化修饰的机制尚未得到详细研究。通过电子顺磁共振(EPR)光谱我们表明,Hb-DNICs 在过氧亚硝酸盐的作用下以剂量依赖的方式被破坏。同时,DNICs 抑制色氨酸和酪氨酸残基的氧化以及羰基衍生物的形成。它们还可以防止血红蛋白亚基之间的共价交联的形成和血红素基团的降解。这些效应可能源于氧合高铁血红素形式被还原,并且它们可能与 DNICs 直接拦截过氧亚硝酸盐和自由基的能力有关,这些自由基是由于其均裂而产生的。这些数据表明,DNICs 可能确保从心肌缺血中得到保护。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d59d/8703631/29c2834ac797/ijms-22-13649-g001.jpg

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