Hoffmann W, Sarzala M G, Chapman D
Proc Natl Acad Sci U S A. 1979 Aug;76(8):3860-4. doi: 10.1073/pnas.76.8.3860.
The rotational motion of the sarcoplasmic reticulum Ca2+-activated ATPase (ATP phosphohydrolase, EC 3.6.1.3) has been investigated by measuring the decay of laser flash-induced dichroism with the covalently attached triplet probe eosin isothiocyanate. The Arrhenius plot for rotational mobility indicates two discontinuities at approximately 15 degrees C and approximately 35 degrees C. The experimental data are rationalized in terms of a sudden conformeric change in the ATPase at 15 degrees C and a temperature-dependent equilibrium existing between the conformationally altered ATPase and oligomeric forms of it in the temperature range 15-35 degrees C. The enzymatic activity, as indicated by a discontinuity in the Arrhenius plot for the rate of ATP hydrolysis, appears to be sensitive only to the change at 15 degrees C. There is a strong correlation between the activation energy below 15 degrees C for rotational motion (33.6 +/- 2.2 kcal/mol) and enzymatic activity (34 +/- 4 kcal/mol).
通过使用共价连接的三重态探针异硫氰酸伊红测量激光闪光诱导的二色性衰减,研究了肌浆网Ca2 + 激活的ATP酶(ATP磷酸水解酶,EC 3.6.1.3)的旋转运动。旋转迁移率的阿累尼乌斯图表明在约15℃和约35℃处有两个不连续点。根据ATP酶在15℃时的突然构象变化以及在15 - 35℃温度范围内构象改变的ATP酶与其寡聚形式之间存在的温度依赖性平衡,对实验数据进行了合理解释。如ATP水解速率的阿累尼乌斯图中的不连续点所示,酶活性似乎仅对15℃时的变化敏感。15℃以下旋转运动的活化能(33.6 +/- 2.2千卡/摩尔)与酶活性(34 +/- 4千卡/摩尔)之间存在很强的相关性。