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Issue 44, 2014
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How protein structure affects redox reactivity: example of Human centrin 2

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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.

Graphical abstract: How protein structure affects redox reactivity: example of Human centrin 2

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Publication details

The article was received on 07 Aug 2014, accepted on 22 Sep 2014 and first published on 23 Sep 2014


Article type: Paper
DOI: 10.1039/C4CP03536D
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Citation: Phys. Chem. Chem. Phys., 2014,16, 24493-24498

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    How protein structure affects redox reactivity: example of Human centrin 2

    A. Et Taouil, E. Brun, P. Duchambon, Y. Blouquit, M. Gilles, E. Maisonhaute and C. Sicard-Roselli, Phys. Chem. Chem. Phys., 2014, 16, 24493
    DOI: 10.1039/C4CP03536D

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