Mechanism of Interaction between Heme Prosthetic Group of Myoglobin and Globin
ZHU Hongxing, WANG Daoying, XU Weimin, SUN Chong, GE Qingfeng, ZHOU Baojing, LIU Xiao
1.College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China; 2.Institute of Agri-Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China; 3.Computational Institute for Molecules and Materials, School of Chemical Engineering, Nanjing University of Science and Technology, Nanjing 210094, China
Abstract：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.
朱宏星，王道营，徐为民，孙 冲，葛庆丰，周宝晶，刘 潇. 肌红蛋白血红素辅基与珠蛋白相互作用机制[J]. 肉类研究, 2020, 34(7): 7-12.
ZHU Hongxing, WANG Daoying, XU Weimin, SUN Chong, GE Qingfeng, ZHOU Baojing, LIU Xiao. Mechanism of Interaction between Heme Prosthetic Group of Myoglobin and Globin. Meat Research, 2020, 34(7): 7-12.
2020, Vol. 34 
