Thiol- and selenol-based peroxidases: Structure and catalytic properties

Página do item simplificado
dc.contributor.authorMenezes, Isabella Silva
dc.contributor.authorFraga, Iuri Fazolin
dc.contributor.authorMascarenhas, Fernando Júnior Rezende
dc.contributor.authorMoraes, Matheus Henrique Morato de
dc.contributor.authorCavalheiro, Raquel Schmitt
dc.contributor.authorAquino, Vinícius Borges de Moura
dc.contributor.authorSantos, Herisson Ferreira dos
dc.contributor.authorMolina, Júlio Cesar [UNESP]
dc.contributor.authorLahr, Francisco Antonio Rocco
dc.contributor.authorChristoforo, André Luis
dc.contributor.institutionUniversidad de la República
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.date.accessioned2023-03-01T20:33:34Z
dc.date.available2023-03-01T20:33:34Z
dc.date.issued2022-01-01
dc.description.abstractThe three families of thiol- or selenol-based peroxidases (peroxiredoxins, Prx; glutathione peroxidases, GPx; and organic hydroperoxide resistance protein/osmotically inducible protein C, Ohr/OsmC) catalyze the reduction of hydroperoxides at the expense of thiol-containing compounds. In Prx, Ohr/OsmC, and some GPx, the catalysis involves a peroxidatic cysteine, while in other GPx, a selenocysteine. Their specificities for reducing and oxidizing substrates are distinct and may reflect their physiological roles. Prx and GPx share the thioredoxin fold common to the proteins belonging to the thioredoxin superfamily. In contrast, Ohr/OsmC present a unique barrel shape α/β fold. Some Prx change their oligomeric state under different conditions, including protein redox state, which is associated with a chaperone function. Ohr/OsmC are dimers and GPx can be monomeric or tetrameric, irrespective of their oxidation state. The mechanisms behind the extraordinary catalytic efficiency of these enzymes in the reduction of hydroperoxides are discussed.en
dc.description.affiliationDepartamento de Bioquímica Centro de Investigaciones Biomédicas (CEINBIO) Universidad de la República
dc.description.affiliationDepartamento de Genética e Biologia Evolutiva Instituto de Biociências Universidade de São Paulo, SP
dc.description.affiliationInstituto de Biociências Universidade Estadual Paulista UNESP, SP
dc.description.affiliationUnespInstituto de Biociências Universidade Estadual Paulista UNESP, SP
dc.format.extent277-305
dc.identifierhttp://dx.doi.org/10.1016/B978-0-323-90219-9.00008-X
dc.identifier.citationRedox Chemistry and Biology of Thiols, p. 277-305.
dc.identifier.doi10.1016/B978-0-323-90219-9.00008-X
dc.identifier.scopus2-s2.0-85137611173
dc.identifier.urihttp://hdl.handle.net/11449/240805
dc.language.isoeng
dc.relation.ispartofRedox Chemistry and Biology of Thiols
dc.sourceScopus
dc.subjectCatalytic mechanism
dc.subjectFatty acid hydroperoxide
dc.subjectGlutathione peroxidase
dc.subjectHydrogen peroxide
dc.subjectLipoperoxidation
dc.subjectOrganic hydroperoxide resistance protein
dc.subjectPeroxidase
dc.subjectPeroxidatic cysteine
dc.subjectPeroxiredoxin
dc.subjectSelenocysteine
dc.titleThiol- and selenol-based peroxidases: Structure and catalytic propertiesen
dc.typeCapítulo de livro

Arquivos

Coleções

Artigos