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Reactivity and selectivity of iminium organocatalysis improved by a protein host

DOI: 10.1002/anie.201806850 DOI Help

Authors: Alexander R Nödling (Cardiff University) , Katarzyna Świderek (Universitat Jaume I) , Raquel Castillo (Universitat Jaume I) , Jonathan W. Hall (Cardiff University) , Antonio Angelastro (Cardiff University) , Louis C. Morrill (Cardiff University) , Yi Jin (Cardiff University) , Yu-hsuan Tsai (Cardiff University) , Vicent Moliner (Universitat Jaume I) , Louis Y. P. Luk (Cardiff University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie International Edition

State: Published (Approved)
Published: July 2018
Diamond Proposal Number(s): 1881

Abstract: There has been growing interest in operating organocatalysis within a supramolecular system as means of controlling reaction reactivity and stereoselectivity. Here, a protein is used as host for iminium catalysis; a pyrrolidine moiety is covalently linked to biotin, introduced to the protein host streptavidin and tested 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‐Å 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 organocatalysis.

Journal Keywords: hybrid catalyst; organocatalysis; computational enzymology; artificial enzyme; supramolecular chemistry

Subject Areas: Chemistry, Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography