How protein structure affects redox reactivity: example of Human centrin 2.
Phys Chem Chem Phys
; 16(44): 24493-8, 2014 Nov 28.
Article
em En
| MEDLINE
| ID: mdl-25308418
ABSTRACT
Electron transfer inside proteins plays a central role in their reactivity and biological functions. Herein, we developed a combined approach by gamma radiolysis and electrochemistry which allowed a deep insight into the reactivity of Human centrin 2, a protein very sensitive to oxidative stress and involved in several key biological processes. This protein bears a single terminal tyrosine and was observed to be extremely sensitive to ionizing radiation sources, leading to a tyrosine dimer. By cyclic voltammetry in the 100-1000 V s(-1) range, its redox potential and dimerization rate could be evaluated. Accordingly, reaction in solution with a redox mediator revealed an efficient catalysis. Finally, protein denaturation by a progressive increase in temperature was proportional to a decrease of dimerization radiolytic yield. Our results thus demonstrated that the protein structure plays a major role in oxidation sensitivity. This leads to meaningful results to understand protein redox reactivity.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Tirosina
/
Proteínas de Ligação ao Cálcio
/
Proteínas de Ciclo Celular
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article