1. Crystallographic snapshot of an arrested intermediate in the biomimetic activation of CO2.
- Author
-
Ackermann SL, Wolstenholme DJ, Frazee C, Deslongchamps G, Riley SH, Decken A, and McGrady GS
- Subjects
- Bicarbonates metabolism, Binding Sites, Biomimetic Materials metabolism, Biomimetics, Carbonic Anhydrases metabolism, Crystallography, X-Ray, Models, Molecular, Quaternary Ammonium Compounds metabolism, Bicarbonates chemistry, Biomimetic Materials chemistry, Carbon Dioxide metabolism, Carbonic Anhydrases chemistry, Quaternary Ammonium Compounds chemistry
- Abstract
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 ., (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Published
- 2015
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