Journal
CHEMICAL SCIENCE
Volume 11, Issue 12, Pages 3236-3240Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0sc00341g
Keywords
-
Categories
Funding
- Leverhulme Trust [RPG-2015-232]
- EPSRC Critical Resource Catalysis Centre for Doctoral training (CRITICAT) [EP/L016419/1]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available