Thermodynamic and spectroscopic study of Cu(II) and Ni(II) binding to bovine serum albumin

被引:115
作者
Zhang, Y [1 ]
Wilcox, DE [1 ]
机构
[1] Dartmouth Coll, Dept Chem, Hanover, NH 03755 USA
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2002年 / 7卷 / 03期
关键词
bovine serum albumin; isothermal titration calorimetry; copper(II) binding; nickel(II) binding;
D O I
10.1007/s00775-001-0302-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The thermodynamics of Cu(II) and N(II) binding to bovine serum albumin (BSA) have been studied by isothermal titration calorimetry (ITC). The Cu(II) binding affinity of the N-terminal protein site is quantitatively higher when the single free thiol, Cys-34, is reduced (mercaptalbumin), compared to when it is oxidized or derivatized with N-ethylmaleimide. This increased affinity is due predominantly to entropic factors. At higher pH (similar to9). when the protein is in the basic (B) form, a second Cu(II) binds with high affinity to albumin with reduced Cys-34. The Cu(II) coordination has been characterized by UV-vis absorption, CD, and EPR spectroscopy, and the spectral data are consistent with thiolate coordination to a tetragonal Cu(II), indicating this is a type 2 copper site with thiolate ligation. Nickel(II) binding to the N-terminal site of BSA is also modulated by the redox/ligation state of Cys-34, with higher Ni(II) affinity for mercaptalbumin, the predominant circulating form of the protein.
引用
收藏
页码:327 / 337
页数:11
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