Peroxynitrite-mediated protein modification

Peroxynitrite-mediated protein modification refers to the chemical alteration of proteins by peroxynitrite (\(\mathrm{ONOO}^-\( ), a highly reactive nitrogen species formed from the reaction between nitric oxide and superoxide. The most prominent modifications include **nitration and dimerization of tyrosine residues**, **oxidation of cysteine thiol groups**, and **oxidation of methionine sulfur groups**. These changes can modulate or inhibit enzymatic activity, disrupt metal-sulfur clusters in proteins, interfere with cellular redox signaling, promote cell damage or death, and alter immune responses. Such modifications are implicated in various pathophysiological conditions including cardiovascular diseases, neurodegeneration, inflammation, and vascular disorders. While these processes are biologically significant—affecting functions such as signal transduction and cell survival—they do not represent classical therapeutic targets like receptors or enzymes but rather post-translational events contributing to disease pathology.[1][2][3][5]

Other names

Peroxynitrite-induced protein modificationProtein tyrosine nitration (context-dependent)Peroxynitrite-mediated oxidative protein modification