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| 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 |
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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.
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HUANG Chunyang, WANG Lingjuan, WANG Zhe, ZHANG Xinxiao, MA Jingjing, YANG Jing, ZOU Ye, WANG Daoying, XU Weimin. A Review of the Impact of Non-Meat Proteins on Myofibrillar Proteins and Meat Quality[J]. Meat Research, 2023, 37(2): 62-67. |
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2020, Vol. 34 
