| Influences of the Hydrophobicity of the Heme－binding Pocket on the Properties and Functions of Cytochrome b5 Mutants |
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| 引用本文： | 甘建华,王韵华,邬键,黄仲贤,夏宗芗.Influences of the Hydrophobicity of the Heme－binding Pocket on the Properties and Functions of Cytochrome b5 Mutants[J].中国化学,2003,21(10):1385-1389. |
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| 作者姓名： | 甘建华 王韵华 邬键 黄仲贤 夏宗芗 |
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| 作者单位： | [1]StateKeyLaboratoryofBioorganicandNaturalProductsChemistry,ShanghaiInstituteofOrganicChemistry,ChineseAcademyofSciences,Shanghai200032,China [2]ChemicalBiologyLaboratory,DepartmentofChemistry,FudanUniversity,Shanghai200433,China |
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| 摘 要： | The mutation sites of the four mutants F35Y, P40V, V45E and V45Y of cytochrome b5 are located at the edge of the heme-binding pocket. The solvent accessible areas of the “pocket inte-rior“ of the four mutants and the wild-type cytochrome b5 have been calculated based on their crystal structures at high resolu-tion. The change in the hydrophobicity of the heme-binding pocket resulting from the mutation can be quantitatively de-scribed using the difference of the solvent accessible area of the “pocket interior“ of each mutant from that of the wild-type cy-tochrome b5. The influences of the hydrophobicity of the heme-binding pocket on the protein stability and redox potential are discussed.
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| 关 键 词： | 疏水性 细胞色素b5 血红素 性质 结构-功能 突变种 |
Influences of the hydrophobicity of the heme‐binding pocket on the properties and functions of cytochrome b5 mutants |
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| Jian‐Hua Gan,Yun‐Hua Wang,Jian Wu,Zhong‐Xian Huang,Zong‐Xiang Xia.Influences of the hydrophobicity of the heme‐binding pocket on the properties and functions of cytochrome b5 mutants[J].Chinese Journal of Chemistry,2003,21(10):1385-1389. |
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| Authors: | Jian‐Hua Gan Yun‐Hua Wang Jian Wu Zhong‐Xian Huang Zong‐Xiang Xia |
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| Abstract: | The mutation sites of the four mutants F35Y, P40V, V45E and V45Y of cytochrome b5 are located at the edge of the hemebinding pocket. The solvent accessible areas of the “pocket interior” of the four mutants and the wild‐type cytochrome b5 have been calculated based on their crystal structures at high resolution. The change in the hydrophobicity of the heme‐binding pocket resulting from the mutation can be quantitatively described using the difference of the solvent accessible area of the “pocket interior” of each mutant from that of the wild‐type cytochrome b5. The influences of the hydrophobicity of the heme‐binding pocket on the protein stability and redox potential are discussed. |
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| Keywords: | cytochrome b5 mutant heme‐binding pocket solvent accessible area hydrophobicity structure‐function relationship |
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