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Proteome‐Wide Survey of Cysteine Oxidation by Using a Norbornene Probe
Author(s) -
Alcock Lisa J.,
Langini Maike,
Stühler Kai,
Remke Marc,
Perkins Michael V.,
Bernardes Gonçalo J. L.,
Chalker Justin M.
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900729
Subject(s) - cysteine , sulfenic acid , oxidative stress , proteome , chemistry , hydrogen peroxide , proteomics , reactive oxygen species , hela , biochemistry , norbornene , oxidative phosphorylation , redox , cell , enzyme , organic chemistry , gene , polymer , monomer
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 oxidised proteins identified in the HeLa cell model represent the first targets of the ROS 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.