z-logo
Premium
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 .

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom