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Nat Chem. 2014 Mar;6(3):222-8. doi: 10.1038/nchem.1842. Epub 2014 Jan 26.

Induced-fit catalysis of corannulene bowl-to-bowl inversion.

Author information

  • 1Center for the Chemistry of Integrated Systems, Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.
  • 2Organic Chemistry Institute (OCI), University of Zürich, Winterthurerstrasse 190, Zürich, CH-8057, Switzerland.
  • 31] Organic Chemistry Institute (OCI), University of Zürich, Winterthurerstrasse 190, Zürich, CH-8057, Switzerland [2] School of Pharmaceutical Science and Technology, Tianjin University (A210/Building 24), 92 Weijin Road, Nankai District, Tianjin, 300072 PRC, China.

Abstract

Stereoelectronic complementarity between the active site of an enzyme and the transition state of a reaction is one of the tenets of enzyme catalysis. This report illustrates the principles of enzyme catalysis (first proposed by Pauling and Jencks) through a well-defined model system that has been fully characterized crystallographically, computationally and kinetically. Catalysis of the bowl-to-bowl inversion processes that pertain to corannulene is achieved by combining ground-state destabilization and transition-state stabilization within the cavity of an extended tetracationic cyclophane. This synthetic receptor fulfils a role reminiscent of a catalytic antibody by stabilizing the planar transition state for the bowl-to-bowl inversion of (ethyl)corannulene (which accelerates this process by a factor of ten at room temperature) by an induced-fit mechanism first formulated by Koshland.

PMID:
24557137
[PubMed - indexed for MEDLINE]
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