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Sulfenic acid chemistry, detection and cellular lifetime
Vinayak Gupta1, Kate S Carroll
1Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458, USA.
Biochimica Et Biophysica Acta
|June 11, 2013
Summary
Protein sulfenic acid modifications are key to cell signaling and are regulated by reactive oxygen species. This review details their chemistry, detection methods, and future research directions for understanding their roles in health and disease.
Area of Science:
- Biochemistry
- Cell Biology
- Chemical Biology
Background:
- Reactive oxygen species (ROS) mediate cysteine sulfenic acid modification, a crucial regulatory mechanism in cellular signaling.
- The stability of protein sulfenic acids depends on the microenvironment and antioxidant activity.
- Various direct and in situ detection techniques for cysteine modifications have been developed.
Purpose of the Study:
- To provide a historical overview of sulfenic acid chemistry and its protein modifications.
- To survey existing detection techniques, discussing their advantages and limitations.
- To cover aspects of sulfenic acid formation, reduction, and chemical trapping.
Main Methods:
- Literature review of sulfenic acid chemistry and detection methods.
- Discussion of protein modification examples.
- Analysis of rates of formation, reduction, and chemical trapping.
Main Results:
- Early chemical models illuminated sulfenic acid reactivity.
- Studies have characterized sulfenic acid formation in proteins.
- Advanced methods enable direct chemical trapping of protein sulfenic acids in cells and tissues.
Conclusions:
- Protein sulfenic acids play increasingly recognized roles in physiology and pathology.
- Further understanding requires novel chemical insights into sulfenic acid-mediated regulation.
- Future research should focus on improving probe reactivity and selectivity for short-lived sulfenic acids and designing targeted inhibitors.
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