Title
Triosephosphate isomerase tyrosine nitration induced by heme–NaNO2–H2O2 or peroxynitrite: Effects of different natural phenolic compounds
Author
Wanxia Gao, Jie Zhao, Hailing Li, Zhonghong Gao
Year
2017
Journal
Journal of Biochemical and Molecular Toxicology
Abstract
Peroxynitrite and heme peroxidases (or heme)–H2O2–NaNO2 system are the two common ways to cause protein tyrosine nitration in vitro, but the effects of antioxidants on reducing these two pathways-induced protein nitration and oxidation are controversial. Both nitrating systems can dose-dependently induce triosephosphate isomerase (TIM) nitration, however, heme–H2O2–NaNO2 was less destructive to protein secondary structures and led to more nitrated tyrosine residue than 3-morpholinosydnonimine hydrochloride (SIN-1, a peroxynitrite donor). Both of desferrioxamine and catechin could inhibit TIM nitration induced by heme–H2O2–NaNO2 and SIN-1 and protein oxidation induced by SIN-1, but promoted heme–H2O2–NaNO2-induced protein oxidation. Moreover, the antagonism of natural phenolic compounds on SIN-1-induced tyrosine nitration was consistent with their radical scavenging ability, but no similar consensus was found in heme–H2O2–NaNO2-induced nitration. Our results indicated that peroxynitrite and heme–H2O2–NaNO2-induced protein nitration was different, and the later one could be a better model for anti-nitration compounds screening.
Instrument
J-810
Keywords
Circular dichroism, Secondary structure, Chemical stability, Biochemistry