"Homogeneous and enzymatic catalyses are in many respects complementary. By anchoring an organometallic catalyst precursor into a host protein, we hoped to create artificial metalloenzymes with properties reminiscent of both areas. To be able to readily deconvolute the influence of the organometallic fragment from the influence of the protein, we want to focus on enantioselective catalysis. Incorporation of an achiral catalyst precursor in the host protein ensures that any level of enantioselection is induce d by the second coordination sphere provided by the protein. Such an approach offers several appealing features: (i) the possibility of dissociating the activity (primarily dictated by the organometallic catalyst precursor) from the selectivity (governed b y the host protein); (ii) the use of orthogonal diversity-generating procedures (molecular biology for the protein optimization as well as parallel synthesis for the organometallic fragment); and (iii) a novel approach to exploit weak interactions in enantioselective homogeneous catalysis. The approach we focus on relies on a non-covalent incorporation (i.e., supramolecular) of the organometallic catalyst precursor in the protein. Since no chemical coupling step is required upon addition of the catalyst precursor to the protein, we reasoned that the integrity of the organometallic species would be warranted. To ensure the localization of the organometallic catalyst precursor within the protein, however, a very strong non-covalent host-guest (i.e., a protein inhibitor) system should be selected."
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