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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 26, Number 7
BKCSDE 26(7)
July 20, 2005 

Thermodynamic Studies on the Interaction of Copper Ions with Carbonic Anhydrase
N. S. Sarraf, S. Mamaghani-Rad, F. Karbassi, A. A. Saboury*
Carbonic anhydrase, Copper, Titration calorimetry, Circular dichroism, Spectrophotometry
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 °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 Cu2+. 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.
1051 - 1056
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