Issue 12, 2011
From the journal:

Dalton Transactions

Comparison between α- and β-carbonic anhydrases: can Zn(His)3(H2O) and Zn(His)(Cys)2(H2O) sites lead to equivalent enzymes?†

Florent Pannetier,a   Gilles Ohanessiana  and  Gilles Frison*a  

* Corresponding authors

a Laboratoire des Mécanismes Réactionnels, Département de Chimie, Ecole Polytechnique and CNRS, 91128 Palaiseau Cedex, France
E-mail: gilles.frison@polytechnique.org
Fax: +33 1 69 33 48 03
Tel: +33 1 69 33 48 34

Abstract

Large models of α- and β-carbonic anhydrases were compared using DFT calculations. They indicate similar acidity of the coordinated water molecule and zinc affinity. This explains their similar mechanism of action, despite the wide difference in their first coordination sphere.

Graphical abstract: Comparison between α- and β-carbonic anhydrases: can Zn(His)3(H2O) and Zn(His)(Cys)2(H2O) sites lead to equivalent enzymes?

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Article information

DOI
https://doi.org/10.1039/C0DT01454K
Article type
Communication
Submitted
22 Oct 2010
Accepted
12 Jan 2011
First published
04 Feb 2011

Dalton Trans., 2011,40, 2696-2698

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Comparison between α- and β-carbonic anhydrases: can Zn(His)3(H2O) and Zn(His)(Cys)2(H2O) sites lead to equivalent enzymes?

F. Pannetier, G. Ohanessian and G. Frison, Dalton Trans., 2011, 40, 2696 DOI: 10.1039/C0DT01454K

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