Artificial metalloenzymes for enantioselective catalysis: recent advances.

Catalysis is the most efficient strategy for the preparation of enantiopure products. Homogeneous and enzymatic catalyses are in many respects complementary in terms of substrate and reaction scope, operating conditions, enantioselection mechanism, etc. In terms of performance optimization, directed evolution methodologies outperform combinatorial ligand libraries. With the aim of combining the best of both homogeneous and enzymatic worlds (e.g. , reaction scope and performance optimization), the field of artificial metalloenzymes has witnessed a revival. The underlying principle of artificial metalloenzymes, relying on the “chemical mutation” of a protein to incorporate a metal-containing fragment, was developed in the late 1970s by Kaiser and Whitesides (Figure 1). Several recent reviews on artificial enzymes exist ; this minireview focuses on the latest developments in artificial metalloenzymes for enantioselective catalysis. The hybrid catalysts presented here are classified according to the nature of the metal fragment–host protein interaction: supramolecular, dative, and covalent. For simplicity (and irrespective of the nature of the metal fragment–host protein interaction), the inclusion symbol “ ” will be used throughout the review to describe artificial metalloenzymes: metal fragment host protein.