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Anion‐π Enzymes

ACS Cent. Sci., Article ASAP
DOI: 10.1021/acscentsci.6b00097
Publication Date (Web): May 23, 2016
 
Yoann Cotelle†‡, Vincent Lebrun†§, Naomi Sakai†‡, Thomas R. Ward*†§, and Stefan Matile*†‡
† National Centre of Competence in Research (NCCR) Molecular Systems Engineering, Basel, Switzerland
‡ Department of Organic Chemistry, University of Geneva, CH-1211 Geneva, Switzerland
§ Department of Chemistry, University of Basel, CH-4056 Basel, Switzerland
 
 http://pubs.acs.org/doi/pdf/10.1021/acscentsci.6b00097

Abstract

Abstract Image
In this report, we introduce artificial enzymes that operate with anion-π interactions, an interaction that is essentially new to nature. The possibility to stabilize anionic intermediates and transition states on an π-acidic surface has been recently demonstrated, using the addition of malonate half thioesters to enolate acceptors as a biologically relevant example. The best chiral anion-π catalysts operate with an addition/decarboxylation ratio of 4:1, but without any stereoselectivity. To catalyze this important but intrinsically disfavored reaction stereoselectively, a series of anion-π catalysts was equipped with biotin and screened against a collection of streptavidin mutants. With the best hit, the S112Y mutant, the reaction occurred with 95% ee and complete suppression of the intrinsically favored side product from decarboxylation. This performance of anion-π enzymes rivals, if not exceeds, that of the best conventional organocatalysts. Inhibition of the S112Y mutant by nitrate but not by bulky anions supports that contributions from anion-π interactions exist and matter, also within proteins. In agreement with docking results, K121 is shown to be essential, presumably to lower the pKa of the tertiary amine catalyst to operate at the optimum pH around 3, that is below the pKa of the substrate. Most importantly, increasing enantioselectivity with different mutants always coincides with increasing rates and conversion, i.e., selective transition-state stabilization.



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