The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE.

TitleThe active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE.
Publication TypeJournal Article
Year of Publication2016
AuthorsPedre, B., L. A. H. van Bergen, A. Palló, L. A. Rosado, V. Tamu Dufe, I. Van Molle, K. Wahni, H. Erdogan, M. Alonso, F. De Proft, and J. Messens
JournalChem Commun (Camb)
Volume52
Issue67
Pagination10293-6
Date Published2016 Aug 11
ISSN1364-548X
KeywordsCatalytic Domain, Kinetics, Molecular Dynamics Simulation, Mycobacterium tuberculosis, Oxidation-Reduction, Peroxides, Peroxiredoxins, Protein Conformation
Abstract

Peroxiredoxins catalyze the reduction of peroxides, a process of vital importance to survive oxidative stress. A nucleophilic cysteine, also known as the peroxidatic cysteine, is responsible for this catalytic process. We used the Mycobacterium tuberculosis alkyl hydroperoxide reductase E (MtAhpE) as a model to investigate the effect of the chemical environment on the specificity of the reaction. Using an integrative structural (R116A - PDB ; F37H - PDB ), kinetic and computational approach, we explain the mutational effects of key residues in its environment. This study shows that the active site residues are specifically oriented to create an environment which selectively favours a reaction with peroxides.

DOI10.1039/c6cc02645a
Alternate JournalChem. Commun. (Camb.)
PubMed ID27471753
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