Recycling of the high valence states of heme proteins by cysteine residues of thimet-oligopeptidase
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
06/06/2014
06/06/2014
01/11/2013
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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. FAPESP (08/04948-0) CNPq UNIFESP UFABC CAPES |
Identificador |
PLOS One, San Francisco : Public Library of Science - PLOS, v. 8, n. 11, p. e79102-1-e79102-16, Nov. 2013 1932-6203 http://www.producao.usp.br/handle/BDPI/45304 10.1371/journal.pone.0079102 |
Idioma(s) |
eng |
Publicador |
Public Library of Science - PLOS San Francisco |
Relação |
PLoS ONE |
Direitos |
openAccess Copyright Ferreira et al. |
Palavras-Chave | #ENZIMAS (ESTUDO) #OLIGOPEPTÍDEOS |
Tipo |
article original article publishedVersion |