对棕色固氮菌-230固氮酶动力学的研究

高等学校化学学报 ›› 1985, Vol. 6 ›› Issue (2): 172.

对棕色固氮菌-230固氮酶动力学的研究

隋德新, 姜涌明, 杨世忱, 赵荧, 陶慰荪

吉林大学化学系固氮组

收稿日期:1983-04-20 出版日期:1985-02-24 发布日期:1985-02-24

The Kinetic Studies of Nitrogenase from A. Vinelandii-230

Shui Dexin, Jiang Yongming, Yang Shichen, Zhao Ying, Tao Weisun

Group of Nitrogen Fixation, Department of chemistry, Jilin University, Changchun

Received:1983-04-20 Online:1985-02-24 Published:1985-02-24

摘要/Abstract

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.

Abstract: We have studied the kinetics of the nitrogenase from A.vinelandii-230 and found that the nitrogenase is an allosteric enzyme.ATPis a positive effector for the nitrogenase while ADPa negative effector for the nitrogenase.ATPbinding 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.

TrendMD:

隋德新, 姜涌明, 杨世忱, 赵荧, 陶慰荪. 对棕色固氮菌-230固氮酶动力学的研究. 高等学校化学学报, 1985, 6(2): 172.

Shui Dexin, Jiang Yongming, Yang Shichen, Zhao Ying, Tao Weisun . The Kinetic Studies of Nitrogenase from A. Vinelandii-230. Chem. J. Chinese Universities, 1985, 6(2): 172.