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

DOI: 10.1039/C6CC02645A DOI Help

Authors: Brandán Pedre (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel) , Laura A. H. Van Bergen (Brussels Center for Redox Biology; Vrije Universiteit Brussel;) , Anna Palló (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel) , Leonardo A. Rosado (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel) , Veronica Tamu Dufe (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel) , Inge Van Molle (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel) , Khadija Wahni (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel) , Huriye Erdogan (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel) , Mercedes Alonso (Vrije Universiteit Brussel) , Frank De Proft (Vrije Universiteit Brussel) , Joris Messens (Structural Biology Research Center, Oxidative Stress Signaling lab; Brussels Center for Redox Biology; Vrije Universiteit Brussel)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chem. Commun. , VOL 52 , PAGES 10293 - 10296

State: Published (Approved)
Published: July 2016

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 4XIH; F37H – PDB 5C04), 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.

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


Instruments: I03-Macromolecular Crystallography

Other Facilities: Soleil