Acta Phys. -Chim. Sin. ›› 1991, Vol. 7 ›› Issue (04): 400-403.doi: 10.3866/PKU.WHXB19910405

• Communication • Previous Articles     Next Articles

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

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