Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 57, Issue 38, Pages 12478-12482Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201806850
Keywords
enzyme models; molecular dynamics; organocatalysis; proteins; supramolecular chemistry
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Funding
- Cardiff University through the Centre of Doctoral Training for Catalysis sabbatical scholarship
- Cardiff School of Chemistry
- Leverhulme Trust [RPG-2017-195]
- Royal Society [RG150466]
- UK's Wellcome Trust [202056/Z/16/Z, 200730/Z/16/Z]
- Spanish Ministerio de Economia y Competitividad [CTQ2015-66223-C2]
- Juan de la Cierva-Incorporacion contract [IJCI-2016-27503]
- Universitat Jaume I [UJI.B2017-31]
- Wellcome Trust [200730/Z/16/Z] Funding Source: Wellcome Trust
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There has been growing interest in performing organocatalysis within a supramolecular system as a means of controlling reaction reactivity and stereoselectivity. Here, a protein is used as a host for iminium catalysis. A pyrrolidine moiety is covalently linked to biotin and introduced to the protein host streptavidin for organocatalytic activity. Whereas in traditional systems stereoselectivity is largely controlled by the substituents added to the organocatalyst, enantiomeric enrichment by the reported supramolecular system is completely controlled by the host. Also, the yield of the model reaction increases over 10-fold when streptavidin is included. A 1.1 angstrom crystal structure of the protein-catalyst complex and molecular simulations of a key intermediate reveal the chiral scaffold surrounding the organocatalytic reaction site. This work illustrates that proteins can be an excellent supramolecular host for driving stereoselective secondary amine organo-catalysis.
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