Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng City, Jiangsu Province 224002, People's Republic of China.
Spectrochim Acta A Mol Biomol Spectrosc. 2012 Feb;86:381-6. doi: 10.1016/j.saa.2011.10.052. Epub 2011 Oct 29.
The interaction between Cr(2)O(7)(2-) and human serum albumin (HSA) was investigated using fluorescence, UV/vis, FT-IR, CD spectroscopy, and molecular modeling method. The experimental results showed that the fluorescence quenching of HSA by Cr(2)O(7)(2-) is a result of the formation of HSA-chromium(VI) complex; static quenching was confirmed to result in the fluorescence quenching. The corresponding thermodynamic parameters showed that the process of binding Cr(2)O(7)(2-) on HSA was a spontaneous molecular interaction procedure. Ionic, H-bonds and van der Waals interactions play a major role in stabilizing the complex. The Cr(2)O(7)(2-) altered the environments of Trp and Tyr residues in HSA.
采用荧光光谱法、紫外-可见吸收光谱法、傅里叶变换红外光谱法、圆二色谱法和分子模拟方法研究了 Cr(2)O(7)(2-)与牛血清白蛋白（HSA）之间的相互作用。实验结果表明，Cr(2)O(7)(2-)对 HSA 的荧光猝灭是形成 HSA-铬(VI)配合物的结果；证实静态猝灭导致荧光猝灭。相应的热力学参数表明，结合 Cr(2)O(7)(2-)在 HSA 上的过程是一个自发的分子相互作用过程。离子、氢键和范德华相互作用在稳定配合物方面起着主要作用。Cr(2)O(7)(2-)改变了 HSA 中色氨酸和酪氨酸残基的环境。
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