物理化学学报 >> 1991, Vol. 7 >> Issue (04): 400-403.doi: 10.3866/PKU.WHXB19910405

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ATP与Fe4S4*络合的31P-NMR研究

吴也凡; 李春芳; 曾定; 洪亮; 林国栋; 蔡启瑞   

  1. 厦门大学生物系,厦门 361005;厦门大学实验中心;厦门大学化学系
  • 收稿日期:1991-02-08 修回日期:1991-04-08 发布日期:1991-08-15
  • 通讯作者: 吴也凡

31P-NMR Studies on Complexation of Fe4S4* with ATP

Wu Ye-Fan; Li Chun-Fang; Zeng Ding; Hong Liang; Lin Guo-Dong; Cai Qi-Rui   

  1. Depratment of Bioloty, Xiamen University, Xiamen 361005; Experiment center, Xiamen University; Department of Chemistry, Xiamen University
  • Received:1991-02-08 Revised:1991-04-08 Published:1991-08-15
  • Contact: Wu Ye-Fan

关键词: ATP, Fe4S4*簇, 络合

Abstract: Chemical modeling studies of ATP driven electron-transfer in Nitrogenase reaction show that adenylate compounds can complex with [Fe_4S_4(SPh)_4]~(2-) cluster, resulting in down field shifting of the ~(31)P NMR peaks of α-、β- and γ-PO_4 about 13.2ppm. 8.3ppm and 28.3ppm, respectively (in its DMF-D_2O(3:2v/v) solution). in down-field shifting of the ~(31)p NMR peaks of a-and β-PO_4 of ADP by about 15.77ppm and 2.71ppm respectively. (in DMF-D_2O (3:2v/v) solution). The above experimental results is quite similar to the observations of Mortenson et al in Fe-protein system. This may be taken as the strong evidence for supporting the view that all of the MgATP and the MgADP can coordinate to the Fe_4S_4~* center of the Fe-protein through the PO_4 groups, rather than other parts of theprotein.

Key words: ATP, Fe4S4* Cluster, Complexation