Crystallographic snapshot of an arrested intermediate in the biomimetic activation of CO2.
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 .
Department of Chemistry, University of New Brunswick, P.O. Box 4400, Fredericton, N.B., E3B 5A3 (Canada).
Sarah L
SL
Ackermann
David J
DJ
Wolstenholme
Chris
C
Frazee
Ghislain
G
Deslongchamps
Sandra H M
SH
Riley
Andreas
A
Decken
G Sean
GS
McGrady
D001639:Bicarbonates / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism; D032701:Biomimetics; D002245:Carbon Dioxide / Q000378:metabolism*; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D000644:Quaternary Ammonium Compounds / Q000737:chemistry* / Q000378:metabolism
D001639:Bicarbonates; D000644:Quaternary Ammonium Compounds; D002245:Carbon Dioxide; C009405:tetrabutylammonium; D002256:Carbonic Anhydrases
biomimetic system; carbon dioxide; carbonic anhydrases; electronic structure; enzyme models