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学科主题: 生命有机化学
题名: X-ray crystallography, CD and kinetic strudies revealed the essence of the abnormal behaviors of the cytochrome b^5 phe35→Tyr mutant
其他题名: X-射线晶体学,园二色散和动力学研究揭示了细胞色素b5的Phe 35Tyr突变的异常行为的本质
作者: Yao P(姚萍) ; Wu J(邬键) ; Wang YH(王韵华) ; Gan JH(甘建华) ; Sun BY(孙炳耘) ; Xia ZX(夏宗芗) ; Huang ZX(黄仲贤)
通讯作者: 夏宗芗
刊名: Eur. J. Biochem.
发表日期: 2002-01-01
卷: 269, 期:17, 页:4287-4296
收录类别: SCI
部门归属: 中国科学院上海有机化学研究所生命有机化学实验室; 复旦大学
英文摘要: Conserved phenylalanine 35 is one of the hydrophobic patch residues on the surface of cytochrome b5(cyt b5). This patch is partially exposed on the surface ofcyt b5 while its buried face is in direct van der Waals' contact with hem b. Residues Phe35 and Phe/Tyr74 also form an aromatic channel with His39, which is one of the axial ligands of heme b. By site-directed mutagenesis we have produced three mutants of cyt b5: Phe35→Tyr, Phe35→Leu, and Phe35→His. We found that of these three mutants, the Phe35→Tyr mutant displays abonrmal properties. The redox potential of the Phe35→Tyr mutant is 66 m V more negative than that of the wild-type cyt b5 and the oxidized Phe35→Tyr mutant is more stable towards thermal and chemical denaturation than wild-type cty b5 and the oxidized Phe35→Tyr mutant is more stable to wards thermal and chemical denaturation than wild-type cty b5. In this study we studied the most interesting mutant, Phe35→Tyr, by X-ray crystallography, thermal denaturation, CD and kinetic studies of heme dissociation to explore the origin of its unusual behaviors, Analysis of crystal structure of the Phe35→Tyr mutant shows that the overall structure of the mutant is basically the same as that of the wild-type protein. However, the introduction of a hydroxyl group in the heme pocket, and the increased ban der Waals' and electrostatic interactions between the side chain of and the heme probably result in enhancement of stability of the Phe35→Tyr mutant, The kinetic difference of the heme trapped by the heme pocket also supports this conclusion. The detailed conformational changes of the proteins in response to heat have been studied by CD for the first time, revealing the existence of the folding intermediate.
语种: 英语
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/23674
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
Yao P,Wu J,Wang YH,et al. X-ray crystallography, CD and kinetic strudies revealed the essence of the abnormal behaviors of the cytochrome b^5 phe35→Tyr mutant[J]. Eur. J. Biochem.,2002,269(17):4287-4296.
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