The interaction between Cu(II) and bovine hemoglobin was investigated by fluorescence and UV-Vis absorption spectroscopy in ionic liquid aqueous two-phase. Synchronous fluorescence spectrum was used to investigate the conformational change of bovine hemoglobin. The results showed that the interaction,which resulted in the fluorescence quenching of bovine hemoglobin,belonged to a static quenching mechanism,the binding constants were 4. 28×103 L · mol-1(298 K) and 3. 65×103 L · mol-1(310K),and the binding sites were 0.8887(298 K) and 0.8339(310 K). The thermodynamic parameters showed that the interaction between Cu( H ) and bovine hemoglobin was mainly driven by electrostatic force. Although Cu( II ) binded with bovine hemoglobin,it scarcely affected the protein conformation, for the hydrophobic environment in the hydrophobic cavity didn t change.%运用荧光光谱和紫外可见吸收光谱,研究了离子液体双水相体系中Cu(Ⅱ)与牛血红蛋白的相互作用；并用同步荧光法探讨了Cu(Ⅱ)对牛血红蛋白(BHb)构象的影响.结果表明,Cu(Ⅱ)对牛血红蛋白产生了荧光猝灭作用,且属于静态猝灭过程；在298K和310K下的结合常数分别为4.28×103L·mol-1和3.65×103L·mol-1、结合位点数分别为0.8887和0.8339;Cu(Ⅱ)与牛血红蛋白之间的相互作用力类型为静电作用力;Cu(Ⅱ)虽然与BHb发生了作用,但没有改变蛋白质疏水腔的疏水环境,对蛋白质的构象影响不大.
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