Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase

Detalhes bibliográficos
Autor(a) principal: Ferreira, Juliana C. [UNIFESP]
Data de Publicação: 2013
Outros Autores: Icimoto, Marcelo Y. [UNIFESP], Marcondes, Marcelo F. [UNIFESP], Oliveira, Vitor [UNIFESP], Nascimento, Otaciro R., Nantes, Iseli L.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://dx.doi.org/10.1371/journal.pone.0079102
http://repositorio.unifesp.br/handle/11600/36909
Resumo: The peptidolytic enzyme THIMET-oligopeptidase (TOP) is able to act as a reducing agent in the peroxidase cycle of myoglobin (Mb) and horseradish peroxidase (HRP). the TOP-promoted recycling of the high valence states of the peroxidases to the respective resting form was accompanied by a significant decrease in the thiol content of the peptidolytic enzyme. EPR (electron paramagnetic resonance) analysis using DBNBS spin trapping revealed that TOP also prevented the formation of tryptophanyl radical in Mb challenged by H2O2. the oxidation of TOP thiol groups by peroxidases did not promote the inactivating oligomerization observed in the oxidation promoted by the enzyme aging. These findings are discussed towards a possible occurrence of these reactions in cells.
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spelling Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-OligopeptidaseThe peptidolytic enzyme THIMET-oligopeptidase (TOP) is able to act as a reducing agent in the peroxidase cycle of myoglobin (Mb) and horseradish peroxidase (HRP). the TOP-promoted recycling of the high valence states of the peroxidases to the respective resting form was accompanied by a significant decrease in the thiol content of the peptidolytic enzyme. EPR (electron paramagnetic resonance) analysis using DBNBS spin trapping revealed that TOP also prevented the formation of tryptophanyl radical in Mb challenged by H2O2. the oxidation of TOP thiol groups by peroxidases did not promote the inactivating oligomerization observed in the oxidation promoted by the enzyme aging. These findings are discussed towards a possible occurrence of these reactions in cells.Universidade Federal de São Paulo, Dept Biofis, São Paulo, BrazilUniv São Paulo, Inst Fis Sao Carlos, Sao Carlos, SP, BrazilUniv Fed ABC, Ctr Ciencias Nat & Humanas, Santo Andre, SP, BrazilUniversidade Federal de São Paulo, Dept Biofis, São Paulo, BrazilWeb of ScienceFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Universidade Federal de São Paulo (UNIFESP)Universidade Federal do ABC (UFABC)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)FAPESP: 2008/04948-0Public Library ScienceUniversidade Federal de São Paulo (UNIFESP)Universidade de São Paulo (USP)Universidade Federal do ABC (UFABC)Ferreira, Juliana C. [UNIFESP]Icimoto, Marcelo Y. [UNIFESP]Marcondes, Marcelo F. [UNIFESP]Oliveira, Vitor [UNIFESP]Nascimento, Otaciro R.Nantes, Iseli L.2016-01-24T14:34:38Z2016-01-24T14:34:38Z2013-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion16application/pdfhttp://dx.doi.org/10.1371/journal.pone.0079102Plos One. San Francisco: Public Library Science, v. 8, n. 11, 16 p., 2013.10.1371/journal.pone.0079102WOS000326499300055.pdf1932-6203http://repositorio.unifesp.br/handle/11600/36909WOS:000326499300055engPlos Oneinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-08-08T02:58:38Zoai:repositorio.unifesp.br/:11600/36909Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-08-08T02:58:38Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
title Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
spellingShingle Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
Ferreira, Juliana C. [UNIFESP]
title_short Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
title_full Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
title_fullStr Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
title_full_unstemmed Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
title_sort Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
author Ferreira, Juliana C. [UNIFESP]
author_facet Ferreira, Juliana C. [UNIFESP]
Icimoto, Marcelo Y. [UNIFESP]
Marcondes, Marcelo F. [UNIFESP]
Oliveira, Vitor [UNIFESP]
Nascimento, Otaciro R.
Nantes, Iseli L.
author_role author
author2 Icimoto, Marcelo Y. [UNIFESP]
Marcondes, Marcelo F. [UNIFESP]
Oliveira, Vitor [UNIFESP]
Nascimento, Otaciro R.
Nantes, Iseli L.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Universidade Federal do ABC (UFABC)
dc.contributor.author.fl_str_mv Ferreira, Juliana C. [UNIFESP]
Icimoto, Marcelo Y. [UNIFESP]
Marcondes, Marcelo F. [UNIFESP]
Oliveira, Vitor [UNIFESP]
Nascimento, Otaciro R.
Nantes, Iseli L.
description The peptidolytic enzyme THIMET-oligopeptidase (TOP) is able to act as a reducing agent in the peroxidase cycle of myoglobin (Mb) and horseradish peroxidase (HRP). the TOP-promoted recycling of the high valence states of the peroxidases to the respective resting form was accompanied by a significant decrease in the thiol content of the peptidolytic enzyme. EPR (electron paramagnetic resonance) analysis using DBNBS spin trapping revealed that TOP also prevented the formation of tryptophanyl radical in Mb challenged by H2O2. the oxidation of TOP thiol groups by peroxidases did not promote the inactivating oligomerization observed in the oxidation promoted by the enzyme aging. These findings are discussed towards a possible occurrence of these reactions in cells.
publishDate 2013
dc.date.none.fl_str_mv 2013-11-01
2016-01-24T14:34:38Z
2016-01-24T14:34:38Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1371/journal.pone.0079102
Plos One. San Francisco: Public Library Science, v. 8, n. 11, 16 p., 2013.
10.1371/journal.pone.0079102
WOS000326499300055.pdf
1932-6203
http://repositorio.unifesp.br/handle/11600/36909
WOS:000326499300055
url http://dx.doi.org/10.1371/journal.pone.0079102
http://repositorio.unifesp.br/handle/11600/36909
identifier_str_mv Plos One. San Francisco: Public Library Science, v. 8, n. 11, 16 p., 2013.
10.1371/journal.pone.0079102
WOS000326499300055.pdf
1932-6203
WOS:000326499300055
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Plos One
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 16
application/pdf
dc.publisher.none.fl_str_mv Public Library Science
publisher.none.fl_str_mv Public Library Science
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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