The protein environment that surrounds metalloenzyme active sites imparts a wide range of effects that facilitate catalysis. Supramolecular supports for homogenous catalysis may model a number of these effects. However, the use of dendrimers or polymers to provide directed second coordination sphere effects is limited by their unpredictable/unstable structures. Foldamers, based on aromatic amide units, have structures that are both highly stable and predictable in a wide range of solvents. These qualities and the modular approach to their synthesis allows for engineering of cavities of defined size with an organized array of functional groups. This project plans to explore the application of foldamers as supramolecular supports for small molecule mimics of metalloenzyme active sites, specifically [FeFe]-hydrogenase, and in doing so develop a new generation of hydrogenase models with a well defined and tunable second coordination sphere. The research involves the in silico design, and chemical synthesis of foldamers that incorporate small molecule models of [FeFe]-hydrogenase. Through electrochemical and variable temperature NMR studies, the effect of the support on the fluxional and electrocatalytic properties of the model complex will be studied. The applicant has experience in the synthesis and characterization of biomimetics of [FeFe]-hydrogenase and the use of supramolecular supports (cyclodextrins) for their encapsulation. Through joining a host lab in France that specializes in the synthesis and structural characterization of aromatic amide foldamers, this expertise in bioinspired catalysts will be transferred via the proposed cooperative work. Additionally the applicant would act as an envoy between the host lab and a group in Germany, with whom the host lab has an established collaboration, for the spectroelectrochemical study of the foldamer complex systems, thus expanding the transfer of knowledge.
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