高等学校化学学报

高等学校化学学报 ›› 2000, Vol. 21 ›› Issue (12): 1913.

• 研究快报 • 上一篇    下一篇

共振喇曼光谱研究稀土离子Er3+对肌红蛋白结构的影响

赵雨1, 徐金泽2, 赵大庆1, 席时权1, 赵冰2, 徐蔚清2   

  1. 1. 稀土化学与物理开放实验室, 中国科学院长春应用化学研究所, 长春 130022;
    2. 吉林大学超分子结构与谱学开放实验室, 长春 130023
  • 收稿日期:2000-07-14 出版日期:2000-12-24 发布日期:2000-12-24
  • 通讯作者: 赵　冰(1964年出生),男,博士,教授,从事分子光谱研究.
  • 基金资助:

    国家自然科学基金(批准号:29633010)资助

Application of Resonance Raman Spectroscopy to Study the Effect of Rare-earth Ion Er3+on Myoglobin

ZHAO Yu1, XU Jin-Ze2, ZHAO Da-Qing1, XI Shi-Quan1, ZHAO Bing2, XU Wei-Qing2   

  1. 1. State Key Laboratoryof Rare Earth Chemistryand Physics, Changchun Instituteof App lied Chemistry, Chinese Academy of Sciences, Changchun 130022, China;
    2. Key Laboratoryf or Supermolecular Structureand Spectroscopy, Jilin University, Changchun 130023, China
  • Received:2000-07-14 Online:2000-12-24 Published:2000-12-24

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关键词: 稀土离子, 肌红蛋白, 氧化态, 自旋态, 共振喇曼光谱

Abstract: The effect of rare earth ion Er3+on myoglobin(Mb) was studied by using Resonance Raman spectroscopy.The results show that with the variation of Er3+concentrations, both the oxidation state and spin state of Mb are sensitive to the perturbation of Er3+. Er3+added to Mb affects the oxidation and spin state synchronously.The structure sensitive groups of Mb are more accessible to the Er3+than other groups.According to the fluorometry and CDspectra studied and our results as mentioned above, we considered that Er3+does not interact with heme directly, and Er3+probably leads to the conformational changes of Mb due to the change of oxidation and spin state of Heme

Key words: Rare-earth ion, Myoglobin, Oxidation state, Spin state, Resonance Raman spectroscopy

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