We investigate the mechanism of multicenter redox enzymes by combining various kinetic techniques, including direct electrochemistry. By “direct electrochemistry”, we mean that the enzyme is adsorbed onto a rotating electrode which is immerged into a solution of the substrate, electron transfer between the enzyme and the electrode is direct, and the activity is simply monitored as a current. The data can be used to gain information about virtually every step in the mechanism.
We work on various redox enzymes, particularly molybdoenzymes and hydrogenases, in collaboration with several biochemistry groups.
We are interested in studying long distance electron transfer in multicenter redox enzymes, the mechanism at the active site of these enzymes, the oxygen sensibility of hydrogenases. We seek to understand the molecular basis of some of the global properties of redox enzymes: this includes catalytic bias, substrate specificity and resistance to chemical stress. We also develop new methodologies that make it possible to use electrochemistry for studying certain steps in the catalytic mechanism of redox enzymes that may be difficult to probe using conventional techniques (such as mass transport along substrate channels).
Funding is provided by the CNRS, the ANR, Aix-Marseille University, the région PACA and the City of Marseilles. We acknowledge support from the Pôle de compétitivité capenergies.
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