Premium
Peroxynitrite‐mediated oxidative protein modifications
Author(s) -
Ischiropoulos Harry,
Al-Mehdi Abu B.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00307-u
Subject(s) - peroxynitrite , chemistry , nitration , superoxide , oxidative stress , oxidative phosphorylation , reactive oxygen species , protein carbonylation , nitrotyrosine , biochemistry , nitric oxide , bovine serum albumin , tryptophan , cysteine , tyrosine , peroxynitrous acid , reactive nitrogen species , hypochlorous acid , amino acid , lipid peroxidation , organic chemistry , nitric oxide synthase , enzyme
Proteins are targets of reactive species and detection of oxidatively modified proteins is often used as an index of oxidative stress. Peroxynitrite is a strong oxidant formed by reaction of nitric oxide with superoxide. Using fatty acid‐free bovine serum albumin as a model we examined peroxynitrite‐mediated protein modifications. The reaction of protein with peroxynitrite resulted in the oxidation of tryptophan and cysteine, in the nitration of tyrosine, in the formation of dityrosine, in the production of 2,4 dinitrophenylhydrazine‐reactive carbonyls and in protein fragmentation. The formation of 3‐nitrotyrosine represents a specific peroxynitrite‐mediated protein modification that is different from modifications mediated by reactive oxygen species.