SIOC 中文
ACS
Adv search

Acta Chimica Sinica ›› 2008, Vol. 66 ›› Issue (10): 1221-1227. Previous Articles     Next Articles

Original Articles

细胞色素b5突变体P40V血红素微环境核磁共振研究

谌章舟1,2，王志强3，吴厚铭2，黄仲贤3，伍晓雄1，曹春阳*,2   

  1. (1华中农业大学 武汉 430070)
    (2中科院上海有机化学研究所 生命有机国家重点实验室 上海 200032)
    (3复旦大学化学系 上海 200433)
  • 投稿日期:2007-12-31 修回日期:2008-03-10 发布日期:2008-05-28
  • 通讯作者: 曹春阳

1H NMR Studies On Heme Microenvironment of Cytochrome b5 Mutant P40V

SHENG, Zhang-Zhou1,2, WANG, Zhi-Qiang3, WU, Hou-Ming2, HUANG, Zhong-Xian3 WU, Xiao-Xiong1, CAO, Chun-Yang*,2   

  1. (1 Huazhong Agricultural University, Wuhan 430070)
    (2 State Key Laboratory of Bio-organic and Natural Product Chemistry, Shanghai Institute of Organic Chemistry, Chinese Acadmey of Sciences, Shanghai 200032)
    (3 Department of Chemistry, Fudan University, Shanghai 200433)
  • Received:2007-12-31 Revised:2008-03-10 Published:2008-05-28
  • Contact: CAO, Chun-Yang

PDF

830

As a main component of respiratory chain in living system, cytochrome b5 is a low spin electron-transfer hemo protein that carries out a variety of important physiological functions and has been extensively studied by biochemical and biophysical methods. To probe the structural and functional importance of the residue Pro40 in the hydrophobic patch of cytochrome b5 surface, this paper studied its mutant P40V by using modern 1D and 2D 1H NMR techniques to examine its heme environment changes resulting from the mutation from P40 to V40.

Key words: cytochrome b5, P40V, heme, NMR