Crystallographic snapshot of an arrested intermediate in the biomimetic activation of CO2
Autor: | Chris Frazee, Sandra H. M. Riley, David J. Wolstenholme, Sarah L. Ackermann, Ghislain Deslongchamps, Andreas Decken, G. Sean McGrady |
---|---|
Rok vydání: | 2014 |
Předmět: |
chemistry.chemical_classification
Models Molecular Binding Sites biology Chemistry Stereochemistry General Medicine General Chemistry Carbon Dioxide Crystallography X-Ray Catalysis Quaternary Ammonium Compounds Bicarbonates Enzyme Biomimetic Materials Biomimetics Carbonic anhydrase biology.protein Binding site Carbonic Anhydrases |
Zdroj: | Angewandte Chemie (International ed. in English). 54(1) |
ISSN: | 1521-3773 |
Popis: | The design of molecular catalysts that mimic the behavior of enzymes is a topical field of activity in emerging technologies, and can lead to an improved understanding of biological systems. Herein, we report how the bulky arms of the cations in [(n C4 H9 )4 N](+) [HCO3 ](-) give rise to a host scaffold that emulates the substrate binding sites in carbonic anhydrase enzymes, affording a unique glimpse of an arrested intermediate in the base-mediated binding and activation of CO2 . |
Databáze: | OpenAIRE |
Externí odkaz: |