Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.

ABSTRACT: Peroxiredoxin 2 (Prdx2) is a thiol peroxidase with an active site Cys (C52) that reacts rapidly with H₂O₂ and other peroxides. The sulfenic acid product condenses with the resolving Cys (C172) to form a disulfide which is recycled by thioredoxin or GSH via mixed disulfide intermediates or undergoes hyperoxidation to the sulfinic acid. C172 lies near the C terminus, outside the active site. It is not established whether structural changes in this region, such as mixed disulfide formation, affect H₂O₂ reactivity. To investigate, we designed mutants to cause minimal (C172S) or substantial (C172D and C172W) structural disruption. Stopped flow kinetics and mass spectrometry showed that mutation to Ser had minimal effect on rates of oxidation and hyper

SUBMITTER: Peskin AV 

PROVIDER: S-EPMC8049995 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature