Peroxynitrite Inactivates Tryptophan Hydroxylase via Sulfhydryl Oxidation COINCIDENT NITRATION OF ENZYME TYROSYL RESIDUES HAS MINIMAL IMPACT ON CATALYTIC ACTIVITY

TL;DR: Peroxynitrite-dependent tyrosine nitration is likely to occur through the initial reaction of peroxyn itrite with carbon dioxide or metal centers leading to secondary nitrating species.

TL;DR: This review attempts to provide a critical description of some of the most common approaches to quantification of nitric oxide, superoxide, hydrogen peroxide, and peroxynitrite, with attention to key issues that may influence the utility of a particular assay when adapted for use in vascular cells and tissues.

TL;DR: The review is aimed to provide an integrated biochemical view on the formation and reactions of peroxynitrite under biologically relevant conditions and the impact of this stealthy oxidant and one of its major footprints, protein NO2Tyr, in the disruption of cellular homeostasis.

TL;DR: This review summarizes the numerous interdependent mechanisms including excitotoxicity, mitochondrial damage and oxidative stress that have been demonstrated to contribute to this terminal damage of methamphetamine and 3,4-methylenedioxymethamphetamine.

TL;DR: The remarkable reactivity of the critical thiol group in GAPDH (Cys-149) toward peroxynitrite, which is one order of magnitude higher than that of previously studied sulfhydryls, indicate that it may constitute a preferential intracellular target for peroxlynitrite.

TL;DR: It is demonstrated that CO2 can alter the course of peroxynitrite-dependent reactions and serve notice that the reactions have physiological significance only if they are shown to occur at physiological concentrations of CO2 and physiological pH; and the peroxyspine-dependent nitration of tyrosine residues or the oxidation of methionine residues of metabolically regulated proteins can seriously compromise their biological function.

TL;DR: It appears that a partial deficit of dopaminergic transmission in wild-type animals does not prevent the development of sensitization to METH, whereas a deficit in nNOS may attenuate this process.

TL;DR: The close agreement between the rate constants obtained from enzyme inactivation and from stopped-flow kinetics experiments suggests that the mechanism of the reaction between peroxynitrite and GSH-Px involves the oxidation of the ionized selenol of the selenocysteine residue in the enzyme's active site (E-Se-) by peroxlynitrite.