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作 者:黎燕 蔡丽玲 王凯 胡亚涛 张秀清 梁福沛 Li Yan;Cai Liling;Wang Kai;Hu Yatao;Zhang Xiuqing;Liang Fupei(College of Chemistry and Bioengineering,Guangxi Key Laboratory of Electrochemical and Magnetochemical Functional Materials,Guilin University of Technology,Guilin 541004,China)
机构地区:[1]桂林理工大学化学与生物工程学院,广西电磁化学功能物质重点实验室,广西桂林541004
出 处:《中国稀土学报》2018年第6期682-691,共10页Journal of the Chinese Society of Rare Earths
基 金:国家自然科学基金项目(61765005);2014年度广西高校科学技术研究项目(ZD2014061);广西电磁化学功能物质重点实验室项目(EMFM20161106)资助.
摘 要:以4'-苯基-2,2':6′,2″-三联吡啶和Sm(NO_3)_3·6H_2O为原料,采用溶剂热法合成一种单核三联吡啶钐配合物[Sm(ptpy)(NO_3)_3 (H_2O)](ptpy=4'-苯基2,2':6′,2″-三联吡啶)。通过单晶和粉末X射线衍射分析、热重分析、元素分析、红外光谱和荧光光谱对其结构、热稳定性和荧光性能等进行了表征。并且采用紫外-可见光谱和荧光光谱研究了[Sm(ptpy)(NO_3)_3(H_2O)]与牛血清白蛋白的相互作用。结果表明:该配合物属正交晶系,Pbca空间群,a=0.87237(5) nm,b=2.17899(15) nm,c=2.45691 (14) nm,α=β=γ=90°。固体荧光光谱表明在340 nm激发下,配合物在565, 598和647 nm处的特征荧光发射可分别归属为Sm3+的4G_(5/2)→6H_(5/2), 4G_(5/2)→6H_(7/2)和4G_(5/2)→6H_(9/2)跃迁。[Sm(ptpy)(NO_3)_3(H_2O)]与牛血清白蛋白相互作用的荧光猝灭方式为静态猝灭,结合常数K为1.10×10~6,结合位点数n为0.73。A mononuclear samarium complex [Sm(ptpy)(NO3)3(H2O)],where ptpy is 4'-phenyl-2,2':6',2"-terpyridine,was synthesized by solvothermal method with ptpy and Sm(NO3)3·6H2O as reactants.The crystal structure and the thermal stability and the fluorescence property of the complex were characterized by single crystal and power X-ray diffraction,thermogravimetrie analysis,elementary analysis,infrared spectroscopy and fluorescence spectroscopy.And the interaction of [Sm(ptpy)(NO3)3(H2O)] with bovine serum albumin was investigated by UV-Vis spectrum and fluorescence spectrum.The result showed that [Sm(ptpy)(NO3)3(H2O)] crystallizes in the orthorhombic space group Pbca with a =0.87237(5)nm,b =2.17899(15)nm,c =2.45691(14)nm,α=β=γ=90°.The solid-state fluorescence spectrum indicated that the characteristic emission bands observed at 565, 598 and 647nm upon excited at 340nm were attributed to the ^4G5/2→^6H5/2,^4G5/2→^6H7/2 and ^4G5/2→^6H9/2 transitions.The way that the complex quenches the fluorescence of bovine serum albumin is static quenching.The binding constant K is 1.10×10^6 and the binding site number n is 0.73.
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