Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue.

Journal article

Protein sulfenic acids are reactive intermediates in the catalytic cycles of many enzymes as well as the in formation of other redox states. Sulfenic acid formation is a reversible post-translational modification with potential for protein regulation. Dimedone (5,5-dimethyl-1,3-cyclohexanedione) is commonly used in vitro to study sulfenation of purified proteins, selectively "tagging" them, allowing monitoring by mass spectrometry. However dimedone is of little use in complex protein mixtures...

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Authors: Charles, R; Schröder, E; May, G; Free, P; Gaffney, P

• Publication status: Published
• Journal: Molecular and cellular proteomics : MCP
• Volume: 6
• Issue: 9
• Pages: 1473-1484
• Publication date: 2007-09-01
• DOI: 10.1074/mcp.m700065-mcp200
• EISSN: 1535-9484
• ISSN: 1535-9476
• Language: English
• Keywords: Biotin; Chromatography, Liquid; Sulfenic Acids; Muscle Cells; Oxidation-Reduction; Horseradish Peroxidase; Animals; Cyclohexanones; Proteomics; Oxygen; Trypsin; Proteins; Oxidative Stress; Hydrogen Peroxide; Rats; Models, Chemical