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Etude structure-fonction de l'hydrogénase à fer et ingénierie du métabolisme de l'hydrogène chez Clostridium acetobutylicum

Abstract : The hydrogenase of Clostridium acetobutylicum catalyses the oxydation of reduced ferredoxin, leading to reduction of protons and dihydrogen formation. Among the three different classes of hydrogenases, the [Fe-Fe] Hydrogenases harbor a very conserved domain (H-Domain) containing the inorganic catalytic site (Cluster H). CaHydA from C. acetobutylicum possesses, in addition, the F-Domain containing four accessory iron-sulfur clusters. The involvement of accessory iron-sulfur cluster of F-Domain on the catalytic capacities of the enzyme has never been assessed. Moreover, which of the two surface iron-sulfur cluster of the F-Domain who interacts with the physiological redox partner ferredoxin is unknown. Different CaHydA mutants enzymes, modified in the Fe-S cluster composition of the F-Domain have been purified, and spectroscopically, biochemically and electrochemically characterized. These mutants enzymes, impaired in their catalytic activity both in solution and wired to an electrode, suggested, for the first time that the Fe-S clusters of the F-Domain have a long-range thermodynamic effect on the H-cluster and modulate enzyme’s functions. Moreover, it has been shown, and confirmed by molecular modelling, that the [2Fe-2S] surface cluster FS2 of the enzyme is the entry point for the electrons coming from the reduced ferredoxin.
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  • HAL Id : tel-01713620, version 1

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Charles Gauquelin. Etude structure-fonction de l'hydrogénase à fer et ingénierie du métabolisme de l'hydrogène chez Clostridium acetobutylicum. Biochimie [q-bio.BM]. INSA de Toulouse, 2017. Français. ⟨NNT : 2017ISAT0018⟩. ⟨tel-01713620⟩

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