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Comp Biochem Physiol C Toxicol Pharmacol. 2007 Jul-Aug;146(1-2):180-93. Epub 2006 Sep 6.

Reactive cysteine in proteins: protein folding, antioxidant defense, redox signaling and more.

Author information

1
Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil. nettoles@ib.usp.br

Abstract

Cysteine plays structural roles in proteins and can also participate in electron transfer reactions, when some structural folds provide appropriated environments for stabilization of its sulfhydryl group in the anionic form, called thiolate (RS(-)). In contrast, sulfhydryl group of free cysteine has a relatively high pK(a) (8,5) and as a consequence is relatively inert for redox reaction in physiological conditions. Thiolate is considerable more powerful as nucleophilic agent than its protonated form, therefore, reactive cysteine are present mainly in its anionic form in proteins. In this review, we describe several processes in which reactive cysteine in proteins take part, showing a high degree of redox chemistry versatility.

PMID:
17045551
DOI:
10.1016/j.cbpc.2006.07.014
[Indexed for MEDLINE]

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