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://repositorio.unifesp.br/handle/11600/36909
http://dx.doi.org/10.1371/journal.pone.0079102
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 Ferreira, Juliana C. [UNIFESP]Icimoto, Marcelo Y. [UNIFESP]Marcondes, Marcelo F. [UNIFESP]Oliveira, Vitor [UNIFESP]Nascimento, Otaciro R.Nantes, Iseli L.Universidade Federal de São Paulo (UNIFESP)Universidade de São Paulo (USP)Universidade Federal do ABC (UFABC)2016-01-24T14:34:38Z2016-01-24T14:34:38Z2013-11-01Plos One. San Francisco: Public Library Science, v. 8, n. 11, 16 p., 2013.1932-6203http://repositorio.unifesp.br/handle/11600/36909http://dx.doi.org/10.1371/journal.pone.0079102WOS000326499300055.pdf10.1371/journal.pone.0079102WOS:000326499300055The 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.Fundação 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)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, BrazilFAPESP: 2008/04948-0Web of Science16engPublic Library SciencePlos OneRecycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidaseinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000326499300055.pdfapplication/pdf2475208${dspace.ui.url}/bitstream/11600/36909/1/WOS000326499300055.pdf0523b889533480f43bf0715f25f0b28cMD51open accessTEXTWOS000326499300055.pdf.txtWOS000326499300055.pdf.txtExtracted texttext/plain54975${dspace.ui.url}/bitstream/11600/36909/2/WOS000326499300055.pdf.txt92409c0d0ca9992aee95cf4df1cda3f2MD52open access11600/369092022-09-27 10:00:01.679open accessoai:repositorio.unifesp.br:11600/36909Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:24:14.317029Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.en.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.institution.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.issued.fl_str_mv 2013-11-01
dc.date.accessioned.fl_str_mv 2016-01-24T14:34:38Z
dc.date.available.fl_str_mv 2016-01-24T14:34:38Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.citation.fl_str_mv Plos One. San Francisco: Public Library Science, v. 8, n. 11, 16 p., 2013.
dc.identifier.uri.fl_str_mv http://repositorio.unifesp.br/handle/11600/36909
http://dx.doi.org/10.1371/journal.pone.0079102
dc.identifier.issn.none.fl_str_mv 1932-6203
dc.identifier.file.none.fl_str_mv WOS000326499300055.pdf
dc.identifier.doi.none.fl_str_mv 10.1371/journal.pone.0079102
dc.identifier.wos.none.fl_str_mv WOS:000326499300055
identifier_str_mv Plos One. San Francisco: Public Library Science, v. 8, n. 11, 16 p., 2013.
1932-6203
WOS000326499300055.pdf
10.1371/journal.pone.0079102
WOS:000326499300055
url http://repositorio.unifesp.br/handle/11600/36909
http://dx.doi.org/10.1371/journal.pone.0079102
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartof.none.fl_str_mv Plos One
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dc.format.none.fl_str_mv 16
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
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