Thermodynamics of metal ion binding. 2. Metal ion binding by carbonic anhydrase variants

Biochemistry
C A DiTusaE J Toone

Abstract

The ability to construct molecular motifs with predictable properties in aqueous solution requires an extensive knowledge of the relationships between structure and energetics. The design of metal binding motifs is currently an area of intense interest in the bioorganic community. To date synthetic motifs designed to bind metal ions lack the remarkable affinities observed in biological systems. To better understand the structural basis of metal ion affinity, we report here the thermodynamics of binding of divalent zinc ions to wild-type and mutant carbonic anhydrases and the interpretation of these parameters in terms of structure. Mutations were made both to the direct His ligand at position 94 and to indirect, or second-shell, ligands Gln-92, Glu-117, and Thr-199. The thermodynamics of ligand binding by several mutant proteins is complicated by the development of a second zinc binding site on mutation; such effects must be considered carefully in the interpretation of thermodynamic data. In all instances modification of the protein produces a complex series of changes in both the enthalpy and entropy of ligand binding. In most cases these effects are most readily rationalized in terms of ligand and protein desolvation, rather...Continue Reading

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Citations

Mar 7, 2003·Journal of Inorganic Biochemistry·Shawn D WettigJeremy S Lee
Jan 11, 2014·The Journal of Physical Chemistry. B·Mathias GruberClaus Hélix-Nielsen
Dec 10, 2013·BMC Biochemistry·Brian F P EdwardsDavid R Evans
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Sep 4, 2015·Biochimica Et Biophysica Acta·Rachel A JohnsonNicholas E Grossoehme
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Mar 13, 2003·Chemical Reviews·Todor Dudev, Carmay Lim
Mar 6, 2003·Journal of the American Chemical Society·Todor DudevCarmay Lim

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