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http://dx.doi.org/10.5012/bkcs.2005.26.7.1051

Thermodynamic Studies on the Interaction of Copper Ions with Carbonic Anhydrase  

Sarraf, N.S. (Institute of Biochemistry and Biophysics, University of Tehran)
Mamaghani-Rad, S. (Institute of Biochemistry and Biophysics, University of Tehran)
Karbassi, F. (Institute of Biochemistry and Biophysics, University of Tehran)
Saboury, A. A. (Institute of Biochemistry and Biophysics, University of Tehran)
Publication Information
Bulletin of the Korean Chemical Society / v.26, no.7, 2005 , pp. 1051-1056 More about this Journal
Abstract
The interaction of bovine carbonic anhydrase II with copper ions was studied by isothermal titration microcalorimetry, circular dichroism, UV spectrophotometry and temperature scanning spectrophotometry methods at 27 ${^{\circ}C}$ in Tris buffer solution at pH = 7.5. It was indicated that there are three non-identical different binding sites on carbonic anhydrase for $Cu^{2+}$. The binding of copper ions is exothermic and can induce some minor changes in the secondary and tertiary structure of the enzyme, which does not unfold it, but can result in a decrease in both activity and stability of the enzyme.
Keywords
Carbonic anhydrase; Copper; Titration calorimetry; Circular dichroism; Spectrophotometry;
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