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Crystallographic snapshot of an arrested intermediate in the biomimetic activation of CO2.
Ackermann, Sarah L; Wolstenholme, David J; Frazee, Chris; Deslongchamps, Ghislain; Riley, Sandra H M; Decken, Andreas; McGrady, G Sean.
Affiliation
  • Ackermann SL; Department of Chemistry, University of New Brunswick, P.O. Box 4400, Fredericton, N.B., E3B 5A3 (Canada).
Angew Chem Int Ed Engl ; 54(1): 164-8, 2015 Jan 02.
Article in En | MEDLINE | ID: mdl-25376525
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 .
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bicarbonates / Carbon Dioxide / Carbonic Anhydrases / Biomimetic Materials / Quaternary Ammonium Compounds Language: En Journal: Angew Chem Int Ed Engl Year: 2015 Document type: Article Country of publication: Germany

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bicarbonates / Carbon Dioxide / Carbonic Anhydrases / Biomimetic Materials / Quaternary Ammonium Compounds Language: En Journal: Angew Chem Int Ed Engl Year: 2015 Document type: Article Country of publication: Germany