Supramolecular catalysis. Part 2: artificial enzyme mimics
Sorbonne Université · Institut Català d'Investigació Química · +2 more institutions
Abstract
The design of artificial catalysts able to compete with the catalytic proficiency of enzymes is an intense subject of research. Non-covalent interactions are thought to be involved in several properties of enzymatic catalysis, notably (i) the confinement of the substrates and the active site within a catalytic pocket, (ii) the creation of a hydrophobic pocket in water, (iii) self-replication properties and (iv) allosteric properties. The origins of the enhanced rates and high catalytic selectivities associated with these properties are still a matter of debate. Stabilisation of the transition state and favourable conformations of the active site and the product(s) are probably part of the answer. We present…
Citation impact
- FWCI
- 33.24
- Percentile
- 100%
- References
- 846
Authors
4- MRMatthieu RaynalCorresponding
Sorbonne Université, Institut Català d'Investigació Química, Institut Parisien de Chimie Moléculaire
- PBPablo Ballester
Institució Catalana de Recerca i Estudis Avançats, Institut Català d'Investigació Química
- AVAnton Vidal‐Ferran
Institut Català d'Investigació Química, Institució Catalana de Recerca i Estudis Avançats
- PWPiet W. N. M. van Leeuwen
Institució Catalana de Recerca i Estudis Avançats, Institut Català d'Investigació Química
Topics & keywords
- Catalysis
- Chemistry
- Supramolecular chemistry
- Artificial enzyme
- Allosteric regulation
- Covalent bond
- Enzyme catalysis
- Active site
- Clean water and sanitation