Final Activity Report Summary - AMEC (Artificial metalloenzymes for enantioselective catalysis) The preparation of enantiomerically pure compounds is one of the most intensively explored areas in organic synthetic chemistry. The field is of great importance for academic research, for the development of new drugs and materials, and, enantioenriched substances are being used in many industrial syntheses of pharmaceutical products and other biologically active substances.In the past three decades, metal-catalysed enantioselective transformations have attained a significant level of expertise and refinement as it was recognised that these are among the most efficient ways to produce enantioenriched materials. This effort was rewarded by the 2001 Nobel Prize in Chemistry, which was shared by Knowles, Noyori, and Sharpless.Nevertheless, despite significant advances, it remains very difficult to predict the outcome of a metal-catalysed asymmetric reaction and, as a consequence, the number of efficient catalysts used for industrial applications remains low.To circumvent the difficulty of predicting the enantioselectivity, combinatorial methodologies have successfully been applied to the discovery and to the elaboration of new chiral catalysts. These studies have shed light on the fact that many subtle experimental parameters often have a significant and unpredictable impact on the outcome of an asymmetric reaction.In recent years, enzymatic catalysis has emerged as an important alternative tool for the synthesis of enantiopure compounds. Again, despite widespread academic and industrial research efforts, the number of industrial biocatalyst applications remains limited.From these considerations, it appears that homogeneous and enzymatic catalyses are in many respects complementary. By grafting well-defined homogeneous catalysts inside a protein cavity, it is expected to create artificial metalloenzymes having properties reminiscent of both fields.The AMEC project aimed at designing homogeneous catalysts that could function either as traditional homogeneous catalysts or as enzymatic catalysts once grafted inside a protein cavity. During the outgoing period in Harvard University (Massachusetts, United States) the researcher developed chiral homobimetallic and heterobimetallic catalysts. The performance of these bioinspired catalysts is reminiscent of natural enzymes, both in terms of selectivity and in terms of activity.