F1-ATP酶的单分子测量揭示了动力冲程与停留持续时间之间的相互依存关系。
Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration.
作者信息
Spetzler David, Ishmukhametov Robert, Hornung Tassilo, Day Lixia Jin, Martin James, Frasch Wayne D
机构信息
School of Life Sciences, Arizona State University, P.O. Box 874501, Tempe, Arizona 85287-4501, USA.
出版信息
Biochemistry. 2009 Aug 25;48(33):7979-85. doi: 10.1021/bi9008215.
Abstract
Increases in the power stroke and dwell durations of single molecules of Escherichia coli F(1)-ATPase were measured in response to viscous loads applied to the motor and inhibition of ATP hydrolysis. The load was varied using different sizes of gold nanorods attached to the rotating gamma subunit and/or by increasing the viscosity of the medium using PEG-400, a noncompetitive inhibitor of ATPase activity. Conditions that increase the duration of the power stroke were found to cause 20-fold increases in the length of the dwell. These results suggest that the order of hydrolysis, product release, and substrate binding may change as the result of external load on the motor or inhibition of hydrolysis.
摘要
在对大肠杆菌F(1)-ATP酶单个分子施加粘性负载以及抑制ATP水解的情况下，测量了其动力冲程和停留持续时间的增加情况。通过将不同尺寸的金纳米棒附着在旋转的γ亚基上和/或使用聚乙二醇-400（一种ATP酶活性的非竞争性抑制剂）增加介质的粘度来改变负载。发现增加动力冲程持续时间的条件会导致停留长度增加20倍。这些结果表明，水解、产物释放和底物结合的顺序可能会因电机上的外部负载或水解抑制而改变。
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