Reactive cysteine in proteins: protein folding, antioxidant defense, redox signaling and more.
Comp Biochem Physiol C Toxicol Pharmacol
; 146(1-2): 180-193, 2007.
Article
em En
| MEDLINE
| ID: mdl-17045551
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredução
/
Transdução de Sinais
/
Proteínas
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Dobramento de Proteína
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Cisteína
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article