不同底物与固氮酶及其钼铁蛋白相互作用的荧光光谱分析

Analysts of Interactions Between Different Substrates and Nitrogenase and Its Mo-Fe Protein by Fluoroscopy

本文研究了不同底物(N_2,H_2,N_2O,NaN_3,C_2H_2)对棕色固氮菌固氮酶及其钼铁蛋白荧光光谱的影响。结果表明,上述底物均能络合在钼铁蛋白及固氮酶上,但络合程度不同,从而为固氮酶系统有多个不同的底物络合中心,底物络合中心在钼铁蛋白分子上,铁蛋白对钼铁蛋白有变构作用,提供了光谱学证据。

The effects of different substrates (N2,H2,N2O,NaN3, and C2H2) on nitrogenase and its Mo-Fe protein from Azotobacter vinelandii-230 have been studied by using fluoroscopy. The results have shown that the substrates mentioned above can all be complexed to the molecules of nitrogenase and its Mo-Fe protein, but complexed are degrees are different,so our data have provided evidences for following points. 1, there are several different sites for substrate complex in the nitrogenase system; 2, the sites for substrate complex are in the Mo-Fe protein molecule, 3, Fe-protein can effect the conformation of Mo-Fe protein.