Stabilization of Labile Carbonyl Addition Intermediates by a Synthetic Receptor
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- 27 July 2007
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 317 (5837) , 493-496
- https://doi.org/10.1126/science.1143272
Abstract
Products of unfavorable chemical equilibria are not readily observed because their high energy and increased reactivity result in low concentrations. Biological macromolecules use binding forces to access unfavorable equilibria and stabilize reactive intermediates by isolating them from the medium. In a similar vein, we describe here a synthetic receptor that allows direct observation of labile tetrahedral intermediates: hemiaminals formed in the reaction of an aldehyde carbonyl group with amines. The receptor encapsulates alkyl-substituted primary amines, then orients them toward a covalently tethered aldehyde function. The hemiaminal intermediates appear at high concentration, confined from the bulk solution and observable at ambient temperature by conventional nuclear magnetic resonance spectroscopy.Keywords
This publication has 21 references indexed in Scilit:
- Molecular Recognition and Stabilization of Iminium Ions in WaterJournal of the American Chemical Society, 2006
- A Reversible Reaction Inside a Self-Assembled CapsuleJournal of the American Chemical Society, 2006
- Direct Crystallographic Observation of a Coordinatively Unsaturated Transition-Metal Complex in situ Generated within a Self-Assembled CageJournal of the American Chemical Society, 2006
- Deep Cavitands Provide Organized Solvation of ReactionsJournal of the American Chemical Society, 2005
- A Deep Cavitand Provides a Structured Environment for the Menschutkin ReactionJournal of the American Chemical Society, 2005
- Mechanism of the Schiff Base Forming Fructose-1,6-bisphosphate Aldolase: Structural Analysis of Reaction IntermediatesBiochemistry, 2005
- Reactivity and Molecular Recognition: Amine Methylation by an Introverted EsterJournal of the American Chemical Society, 2003
- Observation of Covalent Intermediates in an Enzyme Mechanism at Atomic ResolutionScience, 2001
- Enzyme catalysis: not different, just betterNature, 1991
- Free-energy profile for the reaction catalyzed by triosephosphate isomeraseBiochemistry, 1976