所有来源的固氮酶都是钼铁蛋白和铁蛋白两种组分的复合体。所有的固氮酶既能还原分子态氮,还能还原其他一些基质,包括乙炔、氰化物和迭氮化物等。由于固氮酶具有这些突出的特性,因此动力学研究显得十分重要,早就引起国外学者们的注意。要深入研究固氮酶活性部位络合催化的机理,动力学参数是不可缺少的基本资料,然而前几年国外文献报道的数值差别却很大。尤其从固氮酶钼铁蛋白结晶成功之后,尚未见到国内外采用钼铁蛋白结 Nitrogenase from all sources is a complex of the two components of molybdenum ferritin and ferritin. All nitrogenase can not only restore molecular nitrogen, but also reduce some other substrates, including acetylene, cyanide and azide and so on. Due to these prominent features of nitrogenase, kinetic studies have become very important and have long attracted the attention of foreign scholars. It is necessary to further study the mechanism of complex catalysis of the active sites of nitrogenase. Kinetic parameters are indispensable basic data. However, the difference in the numerical values ​​reported in foreign literature a few years ago is quite large. Especially from the nitrogenase Molybdenum ferritin crystallization success has not yet seen the use of molybdenum ferritin junction