Non-covalent allosteric regulation of capsule catalysis |
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Authors: | Vicente Martí-Centelles Rebecca L Spicer Paul J Lusby |
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Institution: | EaStCHEM School of Chemistry, University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh Scotland EH9 3FJ UK, |
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Abstract: | Allosteric regulation is an essential biological process that allows enzymes to modulate their active site properties by binding a control molecule at the protein exterior. Here we show the first example of capsule catalysis in which activity is changed by exotopic binding. This study utilizes a simple Pd2L4 capsule that can partition substrates and external effectors with high fidelity. We also present a detailed, quantitative understanding of how effector interactions alter both substrate and transition state binding. Unlike other allosteric host systems, perturbations are not a consequence of large mechanical changes, rather subtle electronic effects resulting from weak, non-covalent binding to the exterior surface. This investigation paves the way to more sophisticated allosteric systems.External effector binding allosterically regulates the catalytic properties of a simple Pd2L4 capsule. |
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