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• W2999234023 endingPage "66" @default.
• W2999234023 startingPage "55" @default.
• W2999234023 abstract "Abstract Thiol groups in protein cysteine (Cys) residues can undergo one- and two-electron oxidation reactions leading to the formation of thiyl radicals or sulfenic acids, respectively. In this mini-review we summarize the mechanisms and kinetics of the formation of these species by biologically relevant oxidants. Most of the latter react with the deprotonated form of the thiol. Since the pKa of the thiols in protein cysteines are usually close to physiological pH, the thermodynamics and the kinetics of their oxidation in vivo are affected by the acidity of the thiol. Moreover, the protein microenvironment has pronounced effects on cysteine residue reactivity, which in the case of the oxidation mediated by hydroperoxides, is known to confer specificity to particular protein cysteines. Despite their elusive nature, both thiyl radicals and sulfenic acids are involved in the catalytic mechanism of several enzymes and in the redox regulation of protein function and/or signaling pathways. They are usually short-lived species that undergo further reactions that converge in the formation of different stable products, resulting in several post-translational modifications of the protein. Some of these can be reversed through the action of specific cellular reduction systems. Others damage the proteins irreversibly, and can make them more prone to aggregation or degradation." @default.
• W2999234023 created "2020-01-23" @default.
• W2999234023 creator A5010572858 @default.
• W2999234023 creator A5019511328 @default.
• W2999234023 creator A5052410919 @default.
• W2999234023 date "2020-01-10" @default.
• W2999234023 modified "2023-10-01" @default.
• W2999234023 title "Mechanisms and consequences of protein cysteine oxidation: the role of the initial short-lived intermediates" @default.
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• W2999234023 doi "https://doi.org/10.1042/ebc20190053" @default.
• W2999234023 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31919496" @default.

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