Nucleotide binding to creatine kinase: an isothermal titration microcalorimetry study

被引:15
|
作者
Forstner, M
Berger, C
Wallimann, T
机构
[1] ETH Honggerberg, Swiss Fed Inst Technol, Inst Cell Biol, CH-8093 Zurich, Switzerland
[2] Univ Zurich Irchel, Inst Biochem, CH-8057 Zurich, Switzerland
关键词
calorimetry; creatine kinase; domain movement; thermodynamic cycle;
D O I
10.1016/S0014-5793(99)01431-3
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
We investigated the binding of ATP in the presence and absence of Mg2+ to dimeric muscle creatine kinase (CK) by isothermal titration microcalorimetry as a function of pH and temperature. The thermodynamic parameters for these events show that (1) binding of nucleotide to the CK active site does not involve proton exchange with the buffer and (2) the active sites are the only nucleotide binding sites on CK. Interdependence of the active sites in the dimer could not be demonstrated. As CK undergoes major structural changes upon Mg-nucleotide binding, a thermodynamic cycle was employed to calculate the contributions of domain movements to the observed enthalpies. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:111 / 114
页数:4
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