在固氮酶所催化的N_2、C_2H_2等底物还原反应以及ATP水解反应中,固氮酶的钼铁蛋白和铁蛋白各起什么作用,研究这一问题对于阐明固氮酶催化机理有重要的意义。近年来,国内外的研究表明,铁蛋白分子能络合二个MgATP,在Na_2S_2O_4与钼铁蛋白分子之间起传递电子的作用。Mortenson等及Tso等分别用EPR法及凝胶平衡法揭示:钼铁蛋白分子不能络合MgATP。但是,最近Kimber In nitrogenase-catalyzed N 2, C 2 H 2 substrate reduction reaction and ATP hydrolysis reaction, nitrogenase enzyme ferromycins and ferritin each play a role in the study of this issue for clarifying nitrogenase catalytic mechanism has important significance. In recent years, studies at home and abroad show that ferritin can complex two MgATPs and play an electron-transporting role between Na_2S_2O_4 and molybdenum ferritin molecules. Mortenson et al. And Tso et al., Respectively, using the EPR method and the gel balance method revealed that the molybdenum ferritin molecule can not complex MgATP. However, Kimber recently