Torque generation by the Fo motor of the sodium ATPase.
Torque generation by the Fo motor of the sodium ATPase.
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DOI：
10.1529/biophysj.104.042093
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发表时间：
2004-10
影响因子：
3.4
通讯作者：
Jianhua Xing;Hongyun Wang;Christoph von Ballmoos;P. Dimroth;G. Oster
中科院分区：
文献类型：
--
作者：
Jianhua Xing;Hongyun Wang;Christoph von Ballmoos;P. Dimroth;G. Oster
基于最近的结构和功能的研究结果，我们已经构建了一个数学模型的钠驱动的Fo马达的F1 Fo-ATPase从厌氧细菌Propionigenium modestum。该模型揭示了Fo电机的操作的机械化学原理，并解释了所有现有的野生型和突变型Fo电机的实验数据。特别是，该模型预测的ATP水解活性对钠浓度的非单调依赖性，新的实验证实了预测。为了解释实验观察结果，带正电荷的定子残基（R227）必须在ATP合成和水解方向上占据不同的位置。这项工作也说明了如何提取一个电机机制，从动力学实验观察的情况下，完整的结构信息。
Based on recent structural and functional findings, we have constructed a mathematical model for the sodium-driven Fo motor of the F1Fo-ATPase from the anaerobic bacterium Propionigenium modestum. The model reveals the mechanochemical principles underlying the Fo motor's operation, and explains all of the existing experimental data on wild-type and mutant Fo motors. In particular, the model predicts a nonmonotonic dependence of the ATP hydrolysis activity on the sodium concentration, a prediction confirmed by new experiments. To explain experimental observations, the positively charged stator residue (R227) must assume different positions in the ATP synthesis and hydrolysis directions. This work also illustrates how to extract a motor mechanism from dynamical experimental observations in the absence of complete structural information.