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Triosephosphate isomerase tyrosine nitration induced by heme–NaNO 2 –H 2 O 2 or peroxynitrite: Effects of different natural phenolic compounds
Author(s) -
Gao Wanxia,
Zhao Jie,
Li Hailing,
Gao Zhonghong
Publication year - 2017
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21893
Subject(s) - peroxynitrite , nitration , chemistry , heme , tyrosine , hemeprotein , biochemistry , stereochemistry , organic chemistry , enzyme , superoxide
Peroxynitrite and heme peroxidases (or heme)–H 2 O 2 –NaNO 2 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–H 2 O 2 –NaNO 2 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–H 2 O 2 –NaNO 2 and SIN‐1 and protein oxidation induced by SIN‐1, but promoted heme–H 2 O 2 –NaNO 2 ‐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–H 2 O 2 –NaNO 2 ‐induced nitration. Our results indicated that peroxynitrite and heme–H 2 O 2 –NaNO 2 ‐induced protein nitration was different, and the later one could be a better model for anti‐nitration compounds screening.