| Electrostatic effect on electron transfer between cytochrome b5 and cytochrome c |
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| 作者姓名： | HUANG Zhongxian SUN Bingyun WANG Yunhu WANG Wenhu Yao Ping XIE Yi |
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| 作者单位： | Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China |
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| 摘 要： | The binding and electron transfer between wild type, E44A, E56A, E44/56A, E44/48/56A/D60A and F35Y variants of cytochrome b5 and cytochrome c were studied. When mixed with cytochrome c, the cytochrome b, E44/48/56A/D60A did not show the typical UV-vis difference spectrum of absorption, indicating that the alteration of the surface electrostatic potential obviously influenced the spectrum. The electron transfer rates of wild type cytochrome bj, its variants and cytochrome c at different temperature and ionic strength exhibited an order of F35Y > wild type > E56A > E44A > E44/48/56A/D60A. The enthalpy and entropy of the reaction did not change obviously, suggesting that the mutation did not significantly disturb the electron transfer conformation. The investigation of electron transfer rate constants at different ionic strength demonstrated that electrostatic interaction obviously affected the electron transfer process. The significant difference of Cyt b, F35Y and E44/48/56A/D60A from the wild type protein further confirmed the great importance of the electrostatic interaction in the protein electron transfer.
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| 关 键 词： | cytochrome b cytochrome c site-directed mutagenesis electron transfer electrostatic interaction. |
Electrostatic effect on electron transfer between cytochrome b5 and cytochrome c |
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| HUANG Zhongxian,SUN Bingyun,WANG Yunhu,WANG Wenhu,Yao Ping,XIE Yi.Electrostatic effect on electron transfer between cytochrome b5 and cytochrome c[J].Progress in Natural Science,2000,10(5):393-397. |
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| Authors: | HUANG Zhongxian SUN Bingyun WANG Yunhu WANG Wenhu Yao Ping XIE Yi |
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| Institution: | Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China,Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433, China |
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| Abstract: | The binding and electron transfer between wild type, E44A, E56A, E44/56A, E44/48/56A/D60A and F35Y variants of cytochrome b5 and cytochrome c were studied. When mixed with cytochrome c, the cytochrome b, E44/48/56A/D60A did not show the typical UV-vis difference spectrum of absorption, indicating that the alteration of the surface electrostatic potential obviously influenced the spectrum. The electron transfer rates of wild type cytochrome bj, its variants and cytochrome c at different temperature and ionic strength exhibited an order of F35Y > wild type > E56A > E44A > E44/48/56A/D60A. The enthalpy and entropy of the reaction did not change obviously, suggesting that the mutation did not significantly disturb the electron transfer conformation. The investigation of electron transfer rate constants at different ionic strength demonstrated that electrostatic interaction obviously affected the electron transfer process. The significant difference of Cyt b, F35Y and E44/48/56A/D60A from the wild type protein further confirmed the great importance of the electrostatic interaction in the protein electron transfer. |
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| Keywords: | cytochrome b cytochrome c site-directed mutagenesis electron transfer electrostatic interaction |
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