汞(II)与牛血红蛋白相互作用的研究  

Study on the interaction of Hg(II) with BHb

作　　者：张爽[1] 汪涛[1] Fatima 杜林方[1] 

机构地区：[1]四川大学生命科学院生物资源与生物环境教育部重点实验室,四川成都610065

出　　处：《化学研究与应用》2007年第6期611-614,共4页Chemical Research and Application

摘　　要：本文采用紫外光谱(UV/VIS)、荧光光谱和圆二色谱等方法,对汞(II)与牛血红蛋白(BHb)的相互作用进行了研究。结果表明:Hg2+处理导致BHb紫外吸收的增加,出现LMCT带,并随Hg2+浓度的增加LMCT带强度显著增强。BHb分子中Soret带的吸收随着Hg2+作用时间的增加而持续降低,表明Hg2+使部分血红素辅基从BHb中脱离出来。蛋白内源荧光光谱显示,Hg2+与BHb的结合会影响蛋白质的三级结构和四级结构。远紫外圆二色谱表明,Hg2+处理会导致BHb蛋白的α-螺旋含量减少。The interaction between bovine hemoglobin （BHb） and heavy metal ion Hg^2＋ has been investigated under conditions similar to those in vivo by ultraviolet-visible, fluorescence spectra, circular dichroism （CD）. The data from UV spectrometry demonstrated that the binding of Hg^2＋ resulted in remarkable LMCT, indicates the Hg^2＋ binding induces a rearrangement of tertiary structure, which enhances Hg^2＋ site on BHb. The intrinsic fluorescence spectra show that Hg^2＋ affect the tertiary and quaternary structure of BHb, which is supported by the CD data obtained from the near-UV spectra and far-UV spectra. The far-UV spectra shows that the secondary structure was affected by decreasing α-behx content of the protein in the presence of Hg^2＋.

关 键 词：血红蛋白 紫外光谱 荧光光谱 圆二色谱 Hg(Ⅱ) 

分 类 号：O657.3[理学—分析化学]