Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase.

ABSTRACT: Protein-disulfide isomerase (PDI) is a ubiquitous dithiol-disulfide oxidoreductase that performs an array of cellular functions, such as cellular signaling and responses to cell-damaging events. PDI can become dysfunctional by post-translational modifications, including those promoted by biological oxidants, and its dysfunction has been associated with several diseases in which oxidative stress plays a role. Because the kinetics and products of the reaction of these oxidants with PDI remain incompletely characterized, we investigated the reaction of PDI with the biological oxidant peroxynitrite. First, by determining the rate constant of the oxidation of PDI's redox-active Cys residues (Cys⁵³ and Cys³⁹⁷) by hydrogen peroxide (k = 17.3 ± 1.3 m^-1 s

SUBMITTER: Peixoto AS 

PROVIDER: S-EPMC5787819 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature