Proteome-wide survey of cysteine oxidation using a norbornene probe.

Proteome-wide survey of cysteine oxidation using a norbornene probe. Chembiochem. 2019 Dec 04;: Authors: Alcock LJ, Langini M, Stühler K, Remke M, Perkins MV, Bernardes GJL, Chalker JM Abstract Rapid detection of cysteine oxidation in living cells is critical in advancing our understanding of responses to reactive oxygen species (ROS) and oxidative stress. Accordingly, there is a need to develop chemical probes that facilitate proteome-wide detection of cysteine's many oxidation states. Herein, we report the first whole-cell proteomics analysis using a norbornene probe to detect the initial product of cysteine oxidation: cysteine sulfenic acid. The oxidized proteins identified in the HeLa cell model represent the first targets of the reactive oxygen species hydrogen peroxide. The panel of protein hits provides new and important information about the targets of oxidative stress, including 148 new protein members of the sulfenome. These findings provide new leads for the study and understanding of redox signalling and diseases associated with oxidative stress. PMID: 31802583 [PubMed - as supplied by publisher]
Source: Chembiochem - Category: Biochemistry Authors: Tags: Chembiochem Source Type: research