School of Environmental Science and Engineering, Shandong University, 27# Shanda South Road, Jinan 250100, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2010 Jul;76(2):155-60. doi: 10.1016/j.saa.2010.03.006. Epub 2010 Mar 18.
The toxic interaction between Ni(2+) and bovine hemoglobin (BHb) was investigated using fluorescence spectroscopy, synchronous fluorescence spectroscopy, ultraviolet-visible (UV-vis) absorption spectroscopy and circular dichroism spectroscopy (CD) under simulated physiological conditions. The experimental results showed that both dynamic and static quenching occurred simultaneously when Ni(2+) quenched the fluorescence of BHb. The binding site number n, apparent binding constant K(a) and corresponding thermodynamic parameters were measured at different temperatures. There was formation of Ni-BHb complex, but the binding between Ni(2+) and BHb was not strong. The process of the formation of Ni-BHb complex was a spontaneous interaction procedure in which electrostatic interaction played a major role. In addition, UV-vis and CD results showed that the addition of Ni(2+) changed the conformation of BHb.
在模拟生理条件下，使用荧光光谱法、同步荧光光谱法、紫外可见（UV-vis）吸收光谱法和圆二色光谱（CD）研究了 Ni(2+) 和牛血红蛋白（BHb）之间的毒性相互作用。实验结果表明，Ni(2+) 猝灭 BHb 的荧光时，同时发生动态和静态猝灭。在不同温度下测量了结合位点数 n、表观结合常数 K(a) 和相应的热力学参数。形成了 Ni-BHb 配合物，但 Ni(2+) 和 BHb 之间的结合并不牢固。Ni-BHb 配合物的形成过程是一个自发的相互作用过程，其中静电相互作用起主要作用。此外，UV-vis 和 CD 结果表明，Ni(2+) 的加入改变了 BHb 的构象。
