| Texto completo | |
| Autor(es): |
Ferreira, Juliana C.
[1, 2]
;
Icimoto, Marcelo Y.
[1]
;
Marcondes, Marcelo F.
[1]
;
Oliveira, Vitor
[1]
;
Nascimento, Otaciro R.
[3]
;
Nantes, Iseli L.
[2]
Número total de Autores: 6
|
| Afiliação do(s) autor(es): | [1] Univ Fed Sao Paulo, Dept Biofis, Sao Paulo - Brazil
[2] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Santo Andre, SP - Brazil
[3] Univ Sao Paulo, Inst Fis Sao Carlos, Sao Carlos, SP - Brazil
Número total de Afiliações: 3
|
| Tipo de documento: | Artigo Científico |
| Fonte: | PLoS One; v. 8, n. 11 NOV 1 2013. |
| Citações Web of Science: | 2 |
| 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. (AU) | |
| Processo FAPESP: | 08/04948-0 - Estrutura e reatividade de hemoproteínas, hemopeptídeos e porfirinas em meios homogêneos e heterogêneos: aspectos básicos e aplicados à nanotecnologia |
| Beneficiário: | Iseli Lourenço Nantes Cardoso |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |