肌红蛋白血红素辅基与珠蛋白相互作用机制

通过紫外-可见光谱、荧光光谱和分子对接技术研究血红素辅基与珠蛋白相互作用的机制。紫外-可见光谱结果表明,血红素辅基对珠蛋白的二级结构产生了影响;荧光光谱分析表明,血红素辅基与珠蛋白结合生成复合物,产生静态荧光猝灭,288、298、308 K下的结合常数分别为1.497×109、3.818×109、1.327×1010 L/mol,结合位点数为1.87±0.12,血红素辅基对珠蛋白的结合作用力主要是疏水相互作用;同时通过分子对接技术确定了氢键对维持肌红蛋白空间结构的稳定性也极为重要;紫外-可见光谱、荧光光谱和分子对接结果均互相印证。

Mechanism of Interaction between Heme Prosthetic Group of Myoglobin and Globin

In this experiment, the mechanism of the interaction between the heme prosthetic group of myoglobin and globin was studied by means of ultraviolet (UV)-visible spectroscopy, fluorescence spectroscopy and molecular docking. The influence of the hemin prosthetic group on the secondary structure of globin was proved by the UV-visible spectroscopic results. Fluorescence quenching analysis showed that the heme prosthetic group could be combined with globin to form a complex via hydrophobic interaction. The binding constants were 1.497 × 109, 3.818 × 109, and 1.327 × 1010 L/mol at 288, 298 and 308 K, respectively, and the number of binding sites was 1.87 ± 0.12. Molecular docking results further indicated that hydrogen bonding plays a vital role in the spatial structure of myoglobin. All results obtained in this study were consistent with one another.