Metal-Catalyzed Organic Transformations Inside a Protein Scaffold Using Artificial Metalloenzymes

Enzymes catalyze a wide variety of chemical reactions with high selectivity and activity under mild conditions. The research strategy in the construction of artificial metalloenzyme relies on noncovalent attachment of the metal moiety using biotin-(strept)avidin technology. The construction of artificial metalloenzyme can be carried out by anchoring a metal moiety within a protein scaffold with the help of an anchoring group. This chapter presents the results obtained upon applying this strategy toward the generation of artificial metalloenzymes for various enantioselective transformations. The palladium-catalyzed asymmetric allylic alkylation (AAA) is a powerful tool for the elaboration of enantiopure high-added value compounds. The current hypothesis is that proteins with a given catalytic function are difficult to use as host for the creation of artificial metalloenzymes. Proteins which merely act as transporters (myoglobin, serum albumins, (strept)avidin, etc.) may be more suited for the creation of artificial metalloenzymes.