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Mécanisme et spécificité structurale des Méthionine sulfoxyde réductases (Msr) de

Abstract : Methionine sulfoxide reductases (Msr) allow cells to restore function of oxidized proteins on their methionine residues. In the first part, the catalytic mechanism of the MsrA and MsrB of the PilB protein from the bacterial pathogen Neisseria meningitidis has been studied. The two structurally unrelated classes of Msrs display a similar three step catalytic mechanism including the formation of a sulfenic acid intermediate followed by the formation of an intra disulfide bond which is reduced by thioredoxin (Trx). The two classes of Msrs conversely present an opposite stereoselectivity towards the sulfoxide function. In the second part, the three steps of the MsrBs catalytic mechanism have been kinetically characterized. The study of the role of the catalytic amino acid, the characterisation of the MsrB-Trx interaction and, the study of the role of the coordinated metal have also been investigated.
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Contributor : Alexandre Olry <>
Submitted on : Monday, May 30, 2005 - 4:40:06 PM
Last modification on : Friday, February 26, 2021 - 3:02:02 PM
Long-term archiving on: : Friday, November 25, 2016 - 9:11:21 AM


  • HAL Id : tel-00009343, version 1



Alexandre Olry. Mécanisme et spécificité structurale des Méthionine sulfoxyde réductases (Msr) de. Biochimie [q-bio.BM]. Université Henri Poincaré - Nancy I, 2005. Français. ⟨tel-00009343⟩



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