| Studies on Cytochrome c Modified by [PtdienNO_3]Cl |
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| 作者姓名： | 孙自勇 朱德煦 夏志成 槽至灏 唐雯霞 |
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| 作者单位： | Department of Biochemistry，Nanjing University，Nanjing 210008，PRC Department of Biological Science and Medical Engineering，Southeast University，Nanjing 210018，PRC，Department of Biochemistry，Nanjing University，Nanjing 210008，PRC，Coordination Chemistry Institute，Nanjing University，Nanjing 210008，PRC，Biomacromolecule Laboratory，Institute of Biophysics，Academia Sinica，Beijing 100101，PRC，Coordination Chemistry Institute，Nanjing University，Nanjing 210008，PRC，Biomacromolecule Laboratory，Institute of Biophysics，Academia Sinica，Beijing 100101，PRC，Coordination Chemistry Institute，Nanjing University，Nanjing 210008，PRC，Biomacromolecule Laboratory，Institute of Biophysics，Academia Sinica，Beijing 100101，PRC |
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| 基金项目： | Project supported by the National Natural Science Foundation of China and the Bio-macromolecule Laboratory, Institute of Biophysics, Academia Sinica. |
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| 摘 要： | For the first time, PtdienNO_3]Cl was used as a stable reagent to modify ferricytochrome c and the reaction products were separated and purified with the CM-52 cation exchange chromatography. Five components were obtained, corresponding to the native cytochrome c single-labeled, dual-labeled, and triple-labeled derivatives as shown by the analysis of the molar ratio of the two metal atoms (Pt and Fe). The reduction potentials of these proteins were measured by differential pulse voltammetry. His-33 and Trp-59 were identified by~1HNMR as the binding sites of the platinum complex in the modified cytochrome c derivatives. Trp-59 was a conserved amino acid connected with the heme through hydrogen bond, which had not been modified by other transition metal complexes. The platinummodified cytochrome c derivatives might be valuable in exploring the role of the aromatic amino acids, especially Trp-59, in electron transfer.
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Studies on Cytochrome c Modified by [PtdienNO_3]Cl |
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| SUN Zi-Yong ZHU De-Xu.Studies on Cytochrome c Modified by [PtdienNO_3]Cl[J].Science in China(Chemistry),1993(12). |
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| Authors: | SUN Zi-Yong ZHU De-Xu |
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| Abstract: | For the first time, PtdienNO_3]Cl was used as a stable reagent to modify ferricytochrome c and the reaction products were separated and purified with the CM-52 cation exchange chromatography. Five components were obtained, corresponding to the native cytochrome c single-labeled, dual-labeled, and triple-labeled derivatives as shown by the analysis of the molar ratio of the two metal atoms (Pt and Fe). The reduction potentials of these proteins were measured by differential pulse voltammetry. His-33 and Trp-59 were identified by~1HNMR as the binding sites of the platinum complex in the modified cytochrome c derivatives. Trp-59 was a conserved amino acid connected with the heme through hydrogen bond, which had not been modified by other transition metal complexes. The platinummodified cytochrome c derivatives might be valuable in exploring the role of the aromatic amino acids, especially Trp-59, in electron transfer. |
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| Keywords: | cytochrome c [PtdienNO_3]Cl chemical modification HNMR |
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