Structural analysis of zinc-substituted cytochrome c

被引:18
作者
Qian, CM
Yao, Y
Tong, YF
Wang, JF
Tang, WX [1 ]
机构
[1] Nanjing Univ, State Key Lab Coordinat Chem, Nanjing 210093, Peoples R China
[2] Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2003年 / 8卷 / 04期
基金
中国国家自然科学基金;
关键词
Zn cytochrome c; NMR; solution structure; NUCLEAR-MAGNETIC-RESONANCE; ELECTRON-TRANSFER; METALLOCYTOCHROMES-C; PROTEIN STRUCTURES; CRYSTAL-STRUCTURE; SPECTROSCOPY; ABSORPTION; PEROXIDASE; PROGRAM; STEREOCHEMISTRY;
D O I
10.1007/s00775-002-0428-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Zinc-substituted cytochrome c has been widely used in studies of protein-protein interactions and photo-induced electron transfer reactions between proteins. However, the coordination geometry of zinc in zinc-substituted cyt c has not yet been determined; two different opinions about the coordination have been reached. Here the solution structures of zinc-substituted cytochrome c that might be five-coordinated and six-coordinated have been refined separately by using H-1 NMR spectroscopy, and the zinc coordination geometry was determined just by NOE distance constraints. Structural analysis of the energy-minimized average solution structures of both the pentacoordinated and hexacoordinated geometries indicate that that zinc in zinc-substituted cyt c should be bound to both His18 and Met80, which means that the zinc is six-coordinated. RMSD values of the family of 25 six-coordinated structures from the average structure are 0.66+/-0.13 Angstrom and 1.09+/-0.16 Angstrom for the backbone and all heavy atoms, respectively. A statistical analysis of the structure indicates its satisfactory quality. Comparison of the solution structure of the six-coordinated energy-minimized average structure of zinc-substituted cytochrome c with the solution structure of reduced cytochrome c reveals that for the overall folding the secondary structure elements are very close. The availability of the structure provides for a better understanding of the protein-protein complex and for electron transfer processes between Zn cyt c and other metalloprotems.
引用
收藏
页码:394 / 400
页数:7
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