Sulfonation of the resolving cysteine in human peroxiredoxin 1: A comprehensive analysis by mass spectrometry.

ABSTRACT: Peroxiredoxin 1 (Prx1) is an essential peroxidase that reduces cellular peroxides. It holds 2 indispensable cysteines for its activity: a peroxidatic cysteine (C_P) for peroxide reduction and a resolving cysteine (C_R) for C_P regeneration. C_P can be readily sulfonated to C_P-SO₃H by protracted oxidative stress, which inactivates Prx1 as a peroxidase. By comparison, sulfonation of C_R to C_R-SO₃H in mammalian cells has only been reported once. The rare report of C_R sulfonation prompts the following questions: "can C_R-SO₃H be detected more readily with the current high sensitivity mass spectrometers (MS)?" and "do C_P and C_R have distinct propens

SUBMITTER: Wu C 

PROVIDER: S-EPMC5564515 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature