Structure of Cytochromec and Its Platinum-modified Derivatives by Fourier Transform Infrared Spectroscopy

作     者：JIANG Li-juan SUN Wei-yin FANG Jiang-lin SHU Mou-hai TANG Wen-xia 

作者机构：State Key Laboratory of Coordination ChemistryCoor dination Chemistry InstituteNanjing UniversityNanjing210093 Center for Materials AnalysisNanjing UniversityNanjing210093 

出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究(英文版))

年 卷 期：1997年第13卷第2期

页      面：3-11页

核心收录：

学科分类：0710[理学-生物学] 07[理学] 071009[理学-细胞生物学] 09[农学] 0901[农学-作物学] 090102[农学-作物遗传育种] 

主　　题：Cytochrome c Platinum Secondary structure FT IR 

摘      要：The secondary structures of native cytochrome c(cyt c) in both solid and solution states and four platinum modified cyt c derivatives in solution were determined by means of Fourier transform infrared spectroscopy. It was found that the secondary structure of cyt c in solid state is similar to that in the solution. In the cases of platinum modified cyt c derivatives, when the binding sites of platinum complex are on or near the surface of the protein, its secondary structure is similar to that of native cyt c. However, when the platinum complex binds to Met 80 ligand and causes the replacement of the second axial ligand by non native Lys 79 ligand or H 2O supplied by solvent, there is a significant difference between the structures of low or high spin state cyt c derivatives and that of native cyt c. The results suggest that axial ligand Met 80 residue plays an important role in stabilizing the secondary structure of cyt c.