Linked Life Data

17045551

Source:http://linkedlifedata.com/resource/pubmed/id/17045551

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2007-7-30
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1532-0456
pubmed:author
pubmed:issnType
Print
pubmed:volume
146
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
180-93
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:articleTitle
Reactive cysteine in proteins: protein folding, antioxidant defense, redox signaling and more.
pubmed:affiliation
Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil. nettoles@ib.usp.br
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't