Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols

Autores
Zeida, Ari; Trujillo, Madia; Ferrer Sueta, Gerardo; Denicola, Ana; Estrin, Dario Ariel; Radi, Rafael
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Life on Earth evolved in the presence of hydrogen peroxide, and other peroxides also emerged before and with the rise of aerobic metabolism. They were considered only as toxic byproducts for many years. Nowadays, peroxides are also regarded as metabolic products that play essential physiological cellular roles. Organisms have developed efficient mechanisms to metabolize peroxides, mostly based on two kinds of redox chemistry, catalases/peroxidases that depend on the heme prosthetic group to afford peroxide reduction and thiol-based peroxidases that support their redox activities on specialized fast reacting cysteine/selenocysteine (Cys/Sec) residues. Among the last group, glutathione peroxidases (GPxs) and peroxiredoxins (Prxs) are the most widespread and abundant families, and they are the leitmotif of this review. After presenting the properties and roles of different peroxides in biology, we discuss the chemical mechanisms of peroxide reduction by low molecular weight thiols, Prxs, GPxs, and other thiol-based peroxidases. Special attention is paid to the catalytic properties of Prxs and also to the importance and comparative outlook of the properties of Sec and its role in GPxs. To finish, we describe and discuss the current views on the activities of thiol-based peroxidases in peroxide-mediated redox signaling processes.
Fil: Zeida, Ari. Universidad de la República; Uruguay
Fil: Trujillo, Madia. Universidad de la Republica; Uruguay
Fil: Ferrer Sueta, Gerardo. Universidad de la Republica; Uruguay
Fil: Denicola, Ana. Universidad de la Republica; Uruguay
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Radi, Rafael. Universidad de la República; Uruguay
Materia
QM-MM
thiol
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/121625
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Catalysis of Peroxide Reduction by Fast Reacting Protein ThiolsZeida, AriTrujillo, MadiaFerrer Sueta, GerardoDenicola, AnaEstrin, Dario ArielRadi, RafaelQM-MMthiolhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Life on Earth evolved in the presence of hydrogen peroxide, and other peroxides also emerged before and with the rise of aerobic metabolism. They were considered only as toxic byproducts for many years. Nowadays, peroxides are also regarded as metabolic products that play essential physiological cellular roles. Organisms have developed efficient mechanisms to metabolize peroxides, mostly based on two kinds of redox chemistry, catalases/peroxidases that depend on the heme prosthetic group to afford peroxide reduction and thiol-based peroxidases that support their redox activities on specialized fast reacting cysteine/selenocysteine (Cys/Sec) residues. Among the last group, glutathione peroxidases (GPxs) and peroxiredoxins (Prxs) are the most widespread and abundant families, and they are the leitmotif of this review. After presenting the properties and roles of different peroxides in biology, we discuss the chemical mechanisms of peroxide reduction by low molecular weight thiols, Prxs, GPxs, and other thiol-based peroxidases. Special attention is paid to the catalytic properties of Prxs and also to the importance and comparative outlook of the properties of Sec and its role in GPxs. To finish, we describe and discuss the current views on the activities of thiol-based peroxidases in peroxide-mediated redox signaling processes.Fil: Zeida, Ari. Universidad de la República; UruguayFil: Trujillo, Madia. Universidad de la Republica; UruguayFil: Ferrer Sueta, Gerardo. Universidad de la Republica; UruguayFil: Denicola, Ana. Universidad de la Republica; UruguayFil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Radi, Rafael. Universidad de la República; UruguayAmerican Chemical Society2019-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/121625Zeida, Ari; Trujillo, Madia; Ferrer Sueta, Gerardo; Denicola, Ana; Estrin, Dario Ariel; et al.; Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols; American Chemical Society; Chemical Reviews.; 119; 19; 10-2019; 10829-108550009-26651520-6890CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/acs.chemrev.9b00371info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acs.chemrev.9b00371info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:35:53Zoai:ri.conicet.gov.ar:11336/121625instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:35:53.909CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
title Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
spellingShingle Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
Zeida, Ari
QM-MM
thiol
title_short Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
title_full Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
title_fullStr Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
title_full_unstemmed Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
title_sort Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
dc.creator.none.fl_str_mv Zeida, Ari
Trujillo, Madia
Ferrer Sueta, Gerardo
Denicola, Ana
Estrin, Dario Ariel
Radi, Rafael
author Zeida, Ari
author_facet Zeida, Ari
Trujillo, Madia
Ferrer Sueta, Gerardo
Denicola, Ana
Estrin, Dario Ariel
Radi, Rafael
author_role author
author2 Trujillo, Madia
Ferrer Sueta, Gerardo
Denicola, Ana
Estrin, Dario Ariel
Radi, Rafael
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv QM-MM
thiol
topic QM-MM
thiol
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Life on Earth evolved in the presence of hydrogen peroxide, and other peroxides also emerged before and with the rise of aerobic metabolism. They were considered only as toxic byproducts for many years. Nowadays, peroxides are also regarded as metabolic products that play essential physiological cellular roles. Organisms have developed efficient mechanisms to metabolize peroxides, mostly based on two kinds of redox chemistry, catalases/peroxidases that depend on the heme prosthetic group to afford peroxide reduction and thiol-based peroxidases that support their redox activities on specialized fast reacting cysteine/selenocysteine (Cys/Sec) residues. Among the last group, glutathione peroxidases (GPxs) and peroxiredoxins (Prxs) are the most widespread and abundant families, and they are the leitmotif of this review. After presenting the properties and roles of different peroxides in biology, we discuss the chemical mechanisms of peroxide reduction by low molecular weight thiols, Prxs, GPxs, and other thiol-based peroxidases. Special attention is paid to the catalytic properties of Prxs and also to the importance and comparative outlook of the properties of Sec and its role in GPxs. To finish, we describe and discuss the current views on the activities of thiol-based peroxidases in peroxide-mediated redox signaling processes.
Fil: Zeida, Ari. Universidad de la República; Uruguay
Fil: Trujillo, Madia. Universidad de la Republica; Uruguay
Fil: Ferrer Sueta, Gerardo. Universidad de la Republica; Uruguay
Fil: Denicola, Ana. Universidad de la Republica; Uruguay
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Radi, Rafael. Universidad de la República; Uruguay
description Life on Earth evolved in the presence of hydrogen peroxide, and other peroxides also emerged before and with the rise of aerobic metabolism. They were considered only as toxic byproducts for many years. Nowadays, peroxides are also regarded as metabolic products that play essential physiological cellular roles. Organisms have developed efficient mechanisms to metabolize peroxides, mostly based on two kinds of redox chemistry, catalases/peroxidases that depend on the heme prosthetic group to afford peroxide reduction and thiol-based peroxidases that support their redox activities on specialized fast reacting cysteine/selenocysteine (Cys/Sec) residues. Among the last group, glutathione peroxidases (GPxs) and peroxiredoxins (Prxs) are the most widespread and abundant families, and they are the leitmotif of this review. After presenting the properties and roles of different peroxides in biology, we discuss the chemical mechanisms of peroxide reduction by low molecular weight thiols, Prxs, GPxs, and other thiol-based peroxidases. Special attention is paid to the catalytic properties of Prxs and also to the importance and comparative outlook of the properties of Sec and its role in GPxs. To finish, we describe and discuss the current views on the activities of thiol-based peroxidases in peroxide-mediated redox signaling processes.
publishDate 2019
dc.date.none.fl_str_mv 2019-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/121625
Zeida, Ari; Trujillo, Madia; Ferrer Sueta, Gerardo; Denicola, Ana; Estrin, Dario Ariel; et al.; Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols; American Chemical Society; Chemical Reviews.; 119; 19; 10-2019; 10829-10855
0009-2665
1520-6890
CONICET Digital
CONICET
url http://hdl.handle.net/11336/121625
identifier_str_mv Zeida, Ari; Trujillo, Madia; Ferrer Sueta, Gerardo; Denicola, Ana; Estrin, Dario Ariel; et al.; Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols; American Chemical Society; Chemical Reviews.; 119; 19; 10-2019; 10829-10855
0009-2665
1520-6890
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.chemrev.9b00371
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acs.chemrev.9b00371
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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