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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase
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Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase

机译：在分子马达中将构象变化转换为静电能：ATP合酶的能量学

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摘要

F_1-ATPase is the catalytic component of the ATP synthase molecular machine responsible for most of the uphill synthesis of ATP in living systems. The enormous advances in biochemical and structural studies of this machine provide an opportunity for detailed understanding of the nature of its rotary mechanism. However, further quantitative progress in this direction requires development of reliable ways of translating the observed structural changes to the corresponding energies. This requirement is particularly challenging because we are dealing with a large system that couples major structural changes with a chemical process. The present work provides such a structure-function correlation by using the linear response approximation to describe the rotary mechanism. This approach allows one to evaluate the energy of transitions between different conformational states by considering only the changes in the corresponding electrostatic energies of the ligands. The relevant energetics are also obtained by calculating the linear response approximation-based free energies of transferring the ligands from water to the different sites of F_1-ATPase in their different conformational states. We also use the empirical valence bond approach to evaluate the actual free-energy profile for the ATP synthesis in the different conformational states of the system. Integrating the information from the different approaches provides a semiquantitative structure-function correlation for F_1-ATPase. It is found that the conformational changes are converted to changes in the electrostatic interaction between the protein and its ligands, which drives the ATP synthesis.
机译：F_1-ATPase是ATP合酶分子机器的催化成分，负责生物系统中ATP的大部分上坡合成。该机器在生化和结构研究方面的巨大进步为详细了解其旋转机构的性质提供了机会。然而，在这个方向上进一步的定量进展需要开发可靠的方法，将观察到的结构变化转化为相应的能量。这项要求特别具有挑战性，因为我们正在处理一个大型系统，该系统将主要的结构变化与化学过程结合在一起。本工作通过使用线性响应近似来描述旋转机构来提供这种结构-功能相关性。该方法允许通过仅考虑配体的相应静电能的变化来评估不同构象态之间的跃迁能量。还可以通过计算基于线性响应近似的自由能，将配体从水中转移到处于不同构象状态的F_1-ATPase的不同位点，从而获得相关的能量学。我们还使用经验价键方法来评估系统不同构象状态下ATP合成的实际自由能谱。整合来自不同方法的信息为F_1-ATPase提供了半定量的结构-功能相关性。发现构象变化被转换成蛋白质与其配体之间的静电相互作用的变化，这驱动了ATP的合成。

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