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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.
The kinetics study of Azotobacter vinelandian-230 nitrogenase showed that nitrogenase is an allosteric enzyme, ATP is the positive effector of nitrogenase, ADP is the negative effector of nitrogenase and the ATP binding site is nitrogenase Regulatory sites; acetylene reduction active site is the catalytic site of nitrogenase; Av1 and Av2 have two or more binding sites between these binding sites there is a positive synergistic effect, Av1 and Av2 binding sites on the acetylene reduction The active site has a positive synergistic effect.