| 唐乾,张越,曹洪玉,马静,郑学仿,王静云.多种肌红蛋白突变体与Cu(Ⅱ)相互作用机制光谱法研究[J].,2014,54(1):20-27 |
| 多种肌红蛋白突变体与Cu(Ⅱ)相互作用机制光谱法研究 |
| Investigation on mechanism of interaction between Cu(Ⅱ) and multifold mutants of myoglobin by spectroscopic techniques |
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| DOI：10.7511/dllgxb201401004 |
| 中文关键词: 肌红蛋白 突变体(D44K/D60K/K56D) Cu(Ⅱ) 相互作用 光谱法 |
| 英文关键词: myoglobin mutants (D44K/D60K/K56D) Cu(Ⅱ) interaction spectroscopic techniques |
| 基金项目:国家自然科学基金资助项目(21271036)；辽宁省教育厅资助项目(L2013470). |
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| 中文摘要: |
| 运用多种光谱法研究PCR定点突变获得的肌红蛋白突变体(D44K、D60K、K56D)与Cu(Ⅱ)的相互作用．结果表明:Cu(Ⅱ)对突变体的猝灭机理与野生型相同,均为静态猝灭,但结合常数、结合位点数、热力学常数、结合距离以及三维构象方面发生了一些变化．在相同温度下,蛋白与Cu(Ⅱ)的结合能力顺序为Mb(WT) |
| 英文摘要: |
| The interaction between Cu(Ⅱ) and the mutant proteins (D44K, D60K and K56D) which are attained by PCR site-directed mutagenesis is investigated by multi-spectroscopic techniques. The results show that the fluorescence of all the Mbs is quenched regularly with the addition of Cu(Ⅱ).The quenching belongs to the static fluorescence quenching. But the binding constants, the numbers of the binding sites, the thermodynamic parameters, the binding distance and three-dimensional conformation of mutants are different from wild type. At the same temperature, the sequence for binding strength is Mb(WT) |
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