Non-covalent allosteric regulation of capsule catalysis

• Published in: Chemical science (Cambridge) Vol. 11; no. 12; pp. 3236 - 324
• Main Authors: Martí-Centelles, Vicente, Spicer, Rebecca L, Lusby, Paul J
• Format: Journal Article
• Language: English
• Published: Cambridge Royal Society of Chemistry 28.03.2020; The Royal Society of Chemistry
• Subjects: Binding; Biological activity; Catalysis; Chemistry; Crystallography; Substrates
• ISSN: 2041-6520; 2041-6539
• DOI: 10.1039/d0sc00341g

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 Pd 2 L 4 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 Pd 2 L 4 capsule.