摘要
用荧光光谱法研究了三羟基苯基荧光酮(TH-PF)-钼(Ⅵ)配合物与牛血清白蛋白的结合反应。探讨了TH-PF-Mo(Ⅵ)配合物对蛋白质内源荧光的猝灭机理,并测定了不同温度下的结合常数,温度为25℃时,荧光猝灭法测得该反应的结合常数为K=4.78×104L.mol-1,温度为40℃时,荧光猝灭法测得该反应的结合常数为K=3.72×104L.mol-1。根据F rster非辐射能量转移理论,确定了给体-受体之间的作用距离和能量转移效率(E=0.314),并根据热力学参数确定了TH-PF-Mo(Ⅵ)配合物与牛血清白蛋白之间的作用力类型,以静电引力为主。
The mechanism of interaction between bovine serum albumin （BSA） and trihydroxylphenylfluorone（TH-PF）-Mo（Ⅵ） complex in neutral solution was studied by fluorimetrie method. The mechanism of fluorescence quenching of BSA caused by （TH-PF）-Mo（Ⅵ） complex probe was investigated and the binding constants under different temperature were measured. The binding constants of the reaction at 25℃ and 40℃ were calculated by fluorimetrie method to be 4.78× 10^4 L·mol^-1 and 3.72×10^4L·mol^-1 , respectively. According to the theory of Foerster non-radiation energy transfer, the binding distance and transfer efficiency at 25℃ were calculated to he 2.89nm and 0. 314, respectively. Furthermore, the thermodynamic parameters were measured and the results indicated that electrostatic force played a major role in the interaction between TH-PF-Mo（Ⅵ） complex and BSA.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
2006年第10期1899-1902,共4页
Spectroscopy and Spectral Analysis
基金
国家自然科学基金(20577016)
山东省自然科学基金(Y2004B11)
山东省教育厅科技计划(03C05)资助项目
关键词
荧光猝灭
蛋白质
三羟基苯基荧光酮
配合物探针
作用机理
Fluorescence quenching
Protein
Trihydroxylphenylfluorone（TH-PF）-Mo（Ⅵ）
Complex probe
Interaction mechanism
作者简介
黄建华，1954年生，河南科技学院化工系教授
