Structural studies of metalloenzymes and proteins involved in metalloenzyme maturation

Our interests are the study of natural or artificial redox metalloenzymes involved in green processes for the synthesis of biofuels or high-value added molecules. To do that, structural studies are required to understand the maturation of complex metalloenzymes or their reaction mechanism. Our objectives are i) the determination of crystal structures of of several intermediates of the reactions catalyzed by artificial metalloenzymes as well as the structures of hybrids in complex with their substrates. Different aboitic reactions will be studied: sulfoxidation, hydroxylation and carbonation ; ii) the determination of the crystal structure of carbon monoxide dehydrogenas (CODH) and its chaperones, involved in nickel insertion into CODH, as well as the interaction of the enzymes with its gaseous substrates (CO, CO2)