Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/36909
Title: Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase
Authors: 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)
Issue Date: 1-Nov-2013
Publisher: Public Library Science
Citation: Plos One. San Francisco: Public Library Science, v. 8, n. 11, 16 p., 2013.
Abstract: 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.
URI: http://repositorio.unifesp.br/handle/11600/36909
ISSN: 1932-6203
Other Identifiers: http://dx.doi.org/10.1371/journal.pone.0079102
Appears in Collections:Em verificação - Geral

Files in This Item:
File Description SizeFormat 
WOS000326499300055.pdf2.42 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.