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Crystallographic Snapshot of an Arrested Intermediate in the Biomimetic Activation of CO 2
Author(s) -
Ackermann Sarah L.,
Wolstenholme David J.,
Frazee Chris,
Deslongchamps Ghislain,
Riley Sandra H. M.,
Decken Andreas,
McGrady G. Sean
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201407165
Subject(s) - carbonic anhydrase , chemistry , enzyme , substrate (aquarium) , catalysis , carbonic anhydrase ii , stereochemistry , biophysics , combinatorial chemistry , biochemistry , biology , ecology
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 C 4 H 9 ) 4 N] + [HCO 3 ] ‐ 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 CO 2 .