Thermodynamic Studies on the Interaction of Copper Ions with Carbonic Anhydrase

Bulletin of the Korean chemical society

A. A. Saboury¹  S. Mamaghani-Rad¹  N. S. Sarraf¹  F. Karbassi¹ 

关键词: Carbonic anhydrase;    Copper;    Titration calorimetry;    Circular dichroism;    Spectrophotometry;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

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.

【 授权许可】

Unknown