关键词: ATP, Fe₄S_4^*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, Fe₄S_4^* Cluster, Complexation