Recycling of the high valence states of heme proteins by cysteine residues of thimet-oligopeptidase


Autoria(s): Ferreira, Juliana C.; Icimoto, Marcelo Y.; Marcondes, Marcelo F.; Oliveira, Vitor; Nascimento, Otaciro Rangel; Nantes, Iseli L.
Contribuinte(s)

UNIVERSIDADE DE SÃO PAULO

Data(s)

06/06/2014

06/06/2014

01/11/2013

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