Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4786
Title: Influence of outer-shell metal ligands on the structural and electronic properties of horse liver alcohol dehydrogenase zinc active site
Authors: F. L., Gervasio
V., Schettino
Mangani, Stefano 
M., Krack
P., Carloni
M., Parrinello
Keywords: crystal structure; alcohol dehydrogenase; density functional
Issue Date: 2003
Project: None 
Journal: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL
Abstract: 
An analysis of the high resolution 3D structures of zinc enzymes shows that the Zn-His-carboxyl(ate)-HX (X = OH or NH) H-bond motif is common. We investigate here the influence of this motif in the active site of horse liver alcohol dehydrogenase, which features the Zn-His-Asp-H2O motif. Density functional theory calculations are carried out on models of the active site complexed with the NAD+ cofactor, in which the metal ion binds either the alcohol substrate [Bahnson et al. Proc. Nad. Acad. Sci. U. S.A 1997, 94, 1279712802](1) or a water molecule [Meijers et al. J. Biol. Chem. 2001, 276, 9316-9321].(2) Our calculations suggest that in both complexes the presence of Asp49 significantly affects the structural and electronic properties of the metal site. Furthermore, they show that inclusion of the Asp bound water molecule is required to describe the energetics correctly. Finally, they suggest that the Asp49/water pattern could play a role in the enzymatic reaction.
Description: 
47944
URI: http://hdl.handle.net/20.500.12779/4786
ISSN: 1520-6106
DOI: 10.1021/jp027567h
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