【摘要】 对于棕色固氮菌-230固氮酶进行了动力学研究,发现:固氮酶是一种别构酶;ATP是固氮酶的正效应剂;ADP是固氮酶的负效应剂;ATP结合部位是固氮酶的调节部位;乙炔还原活性部位是固氮酶的催化部位;Av1与Av2之间有两个或两个以上的结合部位,这些结合部位之间存在着正协同效应,Av1与Av2的结合部位对乙炔还原活性部位有正协同效应.更多还原

【Abstract】 We have studied the kinetics of the nitrogenase from A. vinelandii-230 and found that the nitrogenase is an allosteric enzyme. ATP is a positive effector for the nitrogenase while ADP a negative effector for the nitrogenase. ATP binding sites are regulatory sites in the nitrogenase and the acetylene reduction active sites are catalytic sites in the nitrogenase. Between Av1 molecules and Av2 molecules, there are two or more than two binding sites among which possesses a positive cooperative effect, namely the effect between the Avl-Av2 binding sites and the acetylene reduction active sites.更多还原