Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng City, Jiangsu Province 224002, People's Republic of China.
J Photochem Photobiol B. 2011 Sep 2;104(3):405-13. doi: 10.1016/j.jphotobiol.2011.04.008. Epub 2011 Apr 29.
The binding interactions of lysozyme with 2-chlorophenol, 2,4-dichlorophenol, 2,4,6-trichlorophenol and pentachlorophenol were investigated by UV-vis absorption, CD, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. The binding constants, quenching mechanism, and the number of binding sites were determined by the quenching of lysozyme fluorescence in presence of chlorophenols. H-bonds and hydrophobic interactions played major roles in stabilizing the chlorophenols-lysozyme complex. The distances r between chlorophenols and lysozyme were calculated to be 1.94nm, 2.75nm, 3.54nm, and 3.76nm for 2-CP, 2,4-DCP, 2,4,6-TCP, and PCP, respectively. The effects of chlorophenols on the conformation of lysozyme were analyzed using CD, synchronous fluorescence and three-dimensional fluorescence spectra.
在生理 pH 值 7.40 下，通过紫外可见吸收、圆二色性、荧光、同步荧光和三维荧光光谱技术研究了溶菌酶与 2-氯苯酚、2,4-二氯苯酚、2,4,6-三氯苯酚和五氯苯酚的结合相互作用。通过在氯苯酚存在下溶菌酶荧光的猝灭，确定了结合常数、猝灭机制和结合位点数。氢键和疏水相互作用在稳定氯苯酚-溶菌酶复合物中起主要作用。计算得到 2-CP、2,4-DCP、2,4,6-TCP 和 PCP 与溶菌酶之间的距离 r 分别为 1.94nm、2.75nm、3.54nm 和 3.76nm。利用圆二色性、同步荧光和三维荧光光谱分析了氯苯酚对溶菌酶构象的影响。
