Rotary coupling mechanism of two nano motors which constitute ATP Synthase

主要结果如下：1)一个调节亚基ε与β结合，并根据膜上质子电化学势的差异改变其构象。2)通过将Trp残基引入到γ亚基上催化部位附近，我们可以阐明明显的负协同作用的来源。3)ATP结合本身驱动酶上水解前的80度阶跃运动。4)使用荧光ATP类似物，我们可以同时直接观察到ATP结合和旋转。我们发现，一旦ATP结合，它就一直保持结合，直到ATP亚单位旋转240度。5)通过使用磁珠和迫使F_1-ATPase沿合成方向旋转，我们可以展示连续的ATP合成。

Major results are as follows.1)A regulatory subunit, ε, binds ATP and it changes its conformation depending on the protonic electrochemical potential difference across the membrane.2)By introducing Trp residue into the vicinity of the catalytic site on β subunits, we could clarify the origin of apparent negative cooperativity.3)ATP binding per se drives 80 degree step motion before hydrolysis on the enzyme.4)By using fluorescent ATP analogue, we could directly observe ATP binding and rotation simultaneously We found that once ATP binds, it remains bound until γ subunit rotates 240 degree.5)By using magnetic beads and forcing F_1-ATPase to rotate in synthetic direction, we could show continuous ATP synthesis.