Etudes cristallographiques d'enzymes impliquées dans les mécanismes de défense contre le stress oxydant : les peptides méthionine sulfoxyde réductases et la NADH rubrédoxine oxydoréductase

Abstract : This work presents the structural analysis by X-Ray crystallography of two families of enzymes involved in defence mechanism against oxidative stress. The first part is dedicated to peptide methionine sulfoxide reductases (Msr) which catalyse methionine sulfoxide (MetSO) reduction. MetSO are formed by oxidation of the methionine residue by oxygen and nitrogen species. Four structures of oxidised and reduced forms of Msr have been solved, in collaboration with the team directed by Pr. G. Branlant in MAEM and with the team of Pr. J.P. Jacquot in IAM, at the UHP Nancy I. The second part of this work was done in collaboration with the laboratory of "Bactéries Gram +" (directed by Pr. H. Petitdemange) at UHP and concerns the NADH rubredoxin oxidoreductase (NROR) from Clostridium acetobutylicum, a solvantogenic anaerobe. The structure of the native form of NROR was solved at 1.01 ÊA resolution. This enzyme was proposed to be involved in the reduction pathway of the superoxide radical.
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Brice Kauffmann. Etudes cristallographiques d'enzymes impliquées dans les mécanismes de défense contre le stress oxydant : les peptides méthionine sulfoxyde réductases et la NADH rubrédoxine oxydoréductase. Autre. Université Henri Poincaré - Nancy 1, 2003. Français. ⟨NNT : 2003NAN10182⟩. ⟨tel-01748177⟩

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