高等学校化学学报 ›› 2002, Vol. 23 ›› Issue (1): 42.

• 研究论文 • 上一篇    下一篇

细胞色素c突变体的共振拉曼光谱研究

郑军伟1, 顾仁敖1, 陆天虹2   

  1. 1. 苏州大学化学系, 苏州 215006;
    2. 中国科学院长春应用化学研究所, 长春 130022
  • 收稿日期:2000-11-15 出版日期:2002-01-24 发布日期:2002-01-24
  • 通讯作者: 郑军伟(1964年出生),男,博士,副教授,从事生物分子拉曼光谱和电化学研究.E-mail:jwzheng@suda.edu.cn E-mail:jwzheng@suda.edu.cn
  • 基金资助:

    国家自然科学基金(批准号:20073028);苏州大学启动基金资助

Resonance Raman Spectroscopic Study of Cytochrome c Mutants

ZHENG Jun-Wei1, GU Ren-Ao1, LU Tian-Hong2   

  1. 1. Department of Chemistry, Suzhou University, Suzhou 215006, China;
    2. Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China
  • Received:2000-11-15 Online:2002-01-24 Published:2002-01-24

摘要: 采用共振拉曼光谱技术研究了细胞色素c一次突变体(WT)及其二次突变体Y67F和N52I在低频区的光谱特征.结果表明,以苯丙氨酸替代WT中酪氨酸残基Tyr67并没有明显影响血红素丙氨酸侧基周围多肽氨基酸残基的构象,而异亮氨酸对天冬酰胺残基Asn52的取代则较大程度地改变了蛋白质内部水分子与周围氨基酸残基间的氢键作用和多肽空腔的疏水性,进而使氨基酸残基和血红素的构象相应发生调变.两种取代都导致形成血红素周围空腔的多肽氨基酸残基构象的变化

关键词: 细胞色素c, 突变, 共振拉曼光谱, 氨基酸构象

Abstract: The spectroscopic characteristics of cytochrome c(WT) and its mutants(Y67F and N52I) in the low frequency region were studied by Resonance Raman technique. The results show that the replacement of phenylalanine for Tyr 67 in WThad a very slight effect on the hydrogen bonding and conformation of the amino acid residues around propionic acid side chains of heme group. However, large effects on the hydrogen bonding of internal water with its surrounding amino acid residues and hydrophobility of the heme cavity were observed as Asn52 was substituted with isoleucine, which resulted in conformational regulations of heme group and surrounding amino acid residues.

Key words: Cytochrome c, Mutation, Resonance Raman spectroscopy, Amino acid conformation

中图分类号: 

TrendMD: