Crystallographic Snapshot of an Arrested Intermediate in the Biomimetic Activation of CO sub(2)

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 sub(4)H sub(9)) sub(4)N] super(+)[HCO sub(3)] su...

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Bibliographic Details
Published in:Angewandte Chemie 2015-01, Vol.127 (1), p.166-170
Main Authors: Ackermann, Sarah L, Wolstenholme, David J, Frazee, Chris, Deslongchamps, Ghislain, Riley, Sandra HM, Decken, Andreas, McGrady, GSean
Format: Article
Language:English
Subjects:
Activation
Binding
Binding sites
Carbon dioxide
Carbonic anhydrase
Catalysis
Cations
Design engineering
Enzymes
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Summary: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 sub(4)H sub(9)) sub(4)N] super(+)[HCO sub(3)] super(-) 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 sub(2).Original Abstract: Die sperrigen Arme des Kations in [(n-C sub(4)H sub(9)) sub(4)N] super(+)[HCO sub(3)] super(-) bilden ein hydrophobes Wirtgeruest, das die Substratbindestellen von Carboanhydrase-Enzymen nachahmt. Daraus ergeben sich einmalige Einblicke in eine Zwischenstufe der basevermittelten CO sub(2)-Bindung und -Aktivierung. In [(n-C sub(4)H sub(9)) sub(4)N] super(+)[HCO sub(3)] super(-) wird die laengste C-O(H)-Bindung fuer nichtkoordiniertes Hydrogencarbonat beobachtet.
ISSN:0044-8249
1521-3757
DOI:10.1002/ange.201407165