Abstract
Design and engineering of protein scaffolds are crucial to create artificial metalloenzymes. Herein we report the first example of C-C bond formation catalyzed by artificial metalloenzymes, which consist of monoclonal antibodies (mAbs) and C2 symmetric metal catalysts. Prepared as a tailored protein scaffold for a binaphthyl derivative (BN), mAbs bind metal catalysts bearing a 1,1′-bi-isoquinoline (BIQ) ligand to yield artificial metalloenzymes. These artificial metalloenzymes catalyze the Friedel-Crafts alkylation reaction. In the presence of mAb R44E1, the reaction proceeds with 88% ee. The reaction catalyzed by Cu-catalyst incorporated into the binding site of mAb R44E1 is found to show excellent enantioselectivity with 99% ee. The protein environment also enables the use of BIQ-based catalysts as asymmetric catalysts for the first time.
Highlights
Artificial metalloenzymes, which consist of transition metal catalysts and biomolecular scaffolds, offer new reactivities or selectivities that are not observed in nature or synthetic catalysts[1,2,3,4,5,6]
Our research focuses on the binaphthyl group as a target molecule to complex with monoclonal antibodies (mAbs). 2,2′-Bis-1,1′-binaphthyl (BINAP) has a unique structure where two phosphine atoms located at the 2,2′ position of the binaphthyl groups play a key role in stabilizing the unique chiral structure and coordination behavior[40,41]
We expect that supramolecular complexation of BIQ-based metal catalysts with mAbs will enhance the diversity of available asymmetric catalysts
Summary
Artificial metalloenzymes, which consist of transition metal catalysts and biomolecular scaffolds, offer new reactivities or selectivities that are not observed in nature or synthetic catalysts[1,2,3,4,5,6]. We report a design strategy for artificial metalloenzymes based on supramolecular complexation of BIQ-based metal catalysts with atroposelective antibodies generated against a structurally simple hapten (Fig. 1b).
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