A critical evaluation of probes for cysteine sulfenic acid

Jasmine M.M. Pople, Justin M. Chalker

Research output: Contribution to journalReview articlepeer-review

5 Citations (Scopus)

Abstract

Cysteine oxidation is important in cellular redox regulation, signaling, and biocatalysis. To understand the biological relevance of cysteine oxidation, it is desirable to identify the proteins involved, the site of the oxidized cysteine, and the relevant oxidation states. Because the thiol of cysteine can be converted to a wide range of oxidation states, mapping these oxidative modifications is challenging. The dynamic and reversible nature of many cysteine oxidation states compounds the difficulty in such proteomic analyses. In this review, we examine methods to detect cysteine sulfenic acid — a particularly challenging functional group to analyze because of its reactive nature. We focus on the selectivity of recently reported probes and discuss some challenges and opportunities in this field.

Original languageEnglish
Pages (from-to)55-65
Number of pages11
JournalCurrent Opinion in Chemical Biology
Volume60
DOIs
Publication statusPublished - Feb 2021
Externally publishedYes

Keywords

  • Cysteine
  • Cysteine oxidation
  • Cysteine sulfenic acid
  • Dimedone
  • Oxidative stress
  • Sulfenamide
  • Sulfenome

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