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

Detalhes bibliográficos
Autor(a) principal: Menezes, Isabella Silva
Data de Publicação: 2022
Outros Autores: Fraga, Iuri Fazolin, Mascarenhas, Fernando Júnior Rezende, Moraes, Matheus Henrique Morato de, Cavalheiro, Raquel Schmitt, Aquino, Vinícius Borges de Moura, Santos, Herisson Ferreira dos, Molina, Júlio Cesar [UNESP], Lahr, Francisco Antonio Rocco, Christoforo, André Luis
Tipo de documento: Capítulo de livro
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/B978-0-323-90219-9.00008-X
http://hdl.handle.net/11449/240805
Resumo: The 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.
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spelling Thiol- and selenol-based peroxidases: Structure and catalytic propertiesCatalytic mechanismFatty acid hydroperoxideGlutathione peroxidaseHydrogen peroxideLipoperoxidationOrganic hydroperoxide resistance proteinPeroxidasePeroxidatic cysteinePeroxiredoxinSelenocysteineThe 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.Departamento de Bioquímica Centro de Investigaciones Biomédicas (CEINBIO) Universidad de la RepúblicaDepartamento de Genética e Biologia Evolutiva Instituto de Biociências Universidade de São Paulo, SPInstituto de Biociências Universidade Estadual Paulista UNESP, SPInstituto de Biociências Universidade Estadual Paulista UNESP, SPUniversidad de la RepúblicaUniversidade de São Paulo (USP)Universidade Estadual Paulista (UNESP)Menezes, Isabella SilvaFraga, Iuri FazolinMascarenhas, Fernando Júnior RezendeMoraes, Matheus Henrique Morato deCavalheiro, Raquel SchmittAquino, Vinícius Borges de MouraSantos, Herisson Ferreira dosMolina, Júlio Cesar [UNESP]Lahr, Francisco Antonio RoccoChristoforo, André Luis2023-03-01T20:33:34Z2023-03-01T20:33:34Z2022-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookPart277-305http://dx.doi.org/10.1016/B978-0-323-90219-9.00008-XRedox Chemistry and Biology of Thiols, p. 277-305.http://hdl.handle.net/11449/24080510.1016/B978-0-323-90219-9.00008-X2-s2.0-85137611173Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengRedox Chemistry and Biology of Thiolsinfo:eu-repo/semantics/openAccess2023-03-01T20:33:34Zoai:repositorio.unesp.br:11449/240805Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T22:46:42.453964Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Thiol- and selenol-based peroxidases: Structure and catalytic properties
title Thiol- and selenol-based peroxidases: Structure and catalytic properties
spellingShingle Thiol- and selenol-based peroxidases: Structure and catalytic properties
Menezes, Isabella Silva
Catalytic mechanism
Fatty acid hydroperoxide
Glutathione peroxidase
Hydrogen peroxide
Lipoperoxidation
Organic hydroperoxide resistance protein
Peroxidase
Peroxidatic cysteine
Peroxiredoxin
Selenocysteine
title_short Thiol- and selenol-based peroxidases: Structure and catalytic properties
title_full Thiol- and selenol-based peroxidases: Structure and catalytic properties
title_fullStr Thiol- and selenol-based peroxidases: Structure and catalytic properties
title_full_unstemmed Thiol- and selenol-based peroxidases: Structure and catalytic properties
title_sort Thiol- and selenol-based peroxidases: Structure and catalytic properties
author Menezes, Isabella Silva
author_facet Menezes, Isabella Silva
Fraga, Iuri Fazolin
Mascarenhas, Fernando Júnior Rezende
Moraes, Matheus Henrique Morato de
Cavalheiro, Raquel Schmitt
Aquino, Vinícius Borges de Moura
Santos, Herisson Ferreira dos
Molina, Júlio Cesar [UNESP]
Lahr, Francisco Antonio Rocco
Christoforo, André Luis
author_role author
author2 Fraga, Iuri Fazolin
Mascarenhas, Fernando Júnior Rezende
Moraes, Matheus Henrique Morato de
Cavalheiro, Raquel Schmitt
Aquino, Vinícius Borges de Moura
Santos, Herisson Ferreira dos
Molina, Júlio Cesar [UNESP]
Lahr, Francisco Antonio Rocco
Christoforo, André Luis
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad de la República
Universidade de São Paulo (USP)
Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv Menezes, Isabella Silva
Fraga, Iuri Fazolin
Mascarenhas, Fernando Júnior Rezende
Moraes, Matheus Henrique Morato de
Cavalheiro, Raquel Schmitt
Aquino, Vinícius Borges de Moura
Santos, Herisson Ferreira dos
Molina, Júlio Cesar [UNESP]
Lahr, Francisco Antonio Rocco
Christoforo, André Luis
dc.subject.por.fl_str_mv Catalytic mechanism
Fatty acid hydroperoxide
Glutathione peroxidase
Hydrogen peroxide
Lipoperoxidation
Organic hydroperoxide resistance protein
Peroxidase
Peroxidatic cysteine
Peroxiredoxin
Selenocysteine
topic Catalytic mechanism
Fatty acid hydroperoxide
Glutathione peroxidase
Hydrogen peroxide
Lipoperoxidation
Organic hydroperoxide resistance protein
Peroxidase
Peroxidatic cysteine
Peroxiredoxin
Selenocysteine
description The 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.
publishDate 2022
dc.date.none.fl_str_mv 2022-01-01
2023-03-01T20:33:34Z
2023-03-01T20:33:34Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/bookPart
format bookPart
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/B978-0-323-90219-9.00008-X
Redox Chemistry and Biology of Thiols, p. 277-305.
http://hdl.handle.net/11449/240805
10.1016/B978-0-323-90219-9.00008-X
2-s2.0-85137611173
url http://dx.doi.org/10.1016/B978-0-323-90219-9.00008-X
http://hdl.handle.net/11449/240805
identifier_str_mv Redox Chemistry and Biology of Thiols, p. 277-305.
10.1016/B978-0-323-90219-9.00008-X
2-s2.0-85137611173
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Redox Chemistry and Biology of Thiols
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 277-305
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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