Dickinson F M
Biochem J. 1985 Jan 1;225(1):159-65. doi: 10.1042/bj2250159.
The dissociation of the aldehyde dehydrogenase X NADH complex was studied by displacement with NAD+. The association reaction of enzyme and NADH was also studied. These processes are biphasic, as shown by McGibbon, Buckley & Blackwell [(1977) Biochem. J. 165, 455-462], but the details of the dissociation reaction are significantly different from those given by those authors. Spectral and kinetic experiments provide evidence for the formation of abortive complexes of the type enzyme X NADH X aldehyde. Kinetic studies at different wavelengths with transcinnamaldehyde as substrate provide evidence for the formation of an enzyme X NADH X cinnamoyl complex. Hydrolysis of the thioester relieves a severe quenching effect on the fluorescence of enzyme-bound NADH.
通过用NAD⁺置换来研究醛脱氢酶与NADH复合物的解离。同时也研究了酶与NADH的缔合反应。如麦吉本、巴克利和布莱克韦尔[（1977年）《生物化学杂志》165卷，455 - 462页]所示，这些过程是双相的，但解离反应的细节与这些作者给出的有显著不同。光谱和动力学实验为酶X NADH X醛类型的流产复合物的形成提供了证据。以反式肉桂醛为底物在不同波长下进行的动力学研究为酶X NADH X肉桂酰复合物的形成提供了证据。硫酯的水解减轻了对酶结合的NADH荧光的严重猝灭作用。
