Proteome-Wide Survey of Cysteine Oxidation by Using a Norbornene Probe

Lisa J. Alcock, Maike Langini, Kai Stühler, Marc Remke, Michael V. Perkins, Gonçalo J.L. Bernardes, Justin M. Chalker

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)1329-1334
Number of pages6
JournalChembiochem
Volume21
Issue number9
DOIs
Publication statusPublished - 4 May 2020

Keywords

  • cysteine oxidation
  • norbornene
  • oxidative stress
  • sulfenic acid
  • sulfenome

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    Alcock, L. J., Langini, M., Stühler, K., Remke, M., Perkins, M. V., Bernardes, G. J. L., & Chalker, J. M. (2020). Proteome-Wide Survey of Cysteine Oxidation by Using a Norbornene Probe. Chembiochem, 21(9), 1329-1334. https://doi.org/10.1002/cbic.201900729