title: Reactive cysteine in proteins: protein folding, antioxidant defense, redox signaling and more.
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.
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil. Electronic address: nettoles@ib.usp.br.
authors.forename: Luis Eduardo Soares
authors.initials: LES
authors.lastname: Netto
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Marcos Antonio
authors.initials: MA
authors.lastname: de Oliveira
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Gisele
authors.initials: G
authors.lastname: Monteiro
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Ana Paula Dias
authors.initials: APD
authors.lastname: Demasi
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: José Renato Rosa
authors.initials: JRR
authors.lastname: Cussiol
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Karen Fulan
authors.initials: KF
authors.lastname: Discola
authors.affiliation: Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo-SP, Brazil.
authors.forename: Marilene
authors.initials: M
authors.lastname: Demasi
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Gustavo Monteiro
authors.initials: GM
authors.lastname: Silva
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Simone Vidigal
authors.initials: SV
authors.lastname: Alves
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Victor Genu
authors.initials: VG
authors.lastname: Faria
authors.affiliation: Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo-SP, Brazil.
authors.forename: Bruno Brasil
authors.initials: BB
authors.lastname: Horta
mesh_terms: D000818:Animals; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism; D006801:Humans; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*; D013879:Thioredoxins / Q000378:metabolism
chemical_list: D011506:Proteins; D013879:Thioredoxins; D005978:Glutathione; D003545:Cysteine