F1Fo ATP synthases produce most of the ATP in the cell. F-type ATP synthases have been investigated for more than 50 years, but a full understanding of their molecular mechanisms has become possible only with the recent structures of complete, functionally competent complexes determined by electron cryo-microscopy (cryo-EM). High-resolution cryo-EM structures offer a wealth of unexpected new insights. The catalytic F1 head rotates with the central γ-subunit for the first part of each ATP-generating power stroke. Joint rotation is enabled by subunit δ/OSCP acting as a flexible hinge between F1 and the peripheral stalk. Subunit a conducts protons to and from the c-ring rotor through two conserved aqueous channels. The channels are separated by ∼6 Å in the hydrophobic core of Fo, resulting in a strong local field that generates torque to drive rotary catalysis in F1. The structure of the chloroplast F1Fo complex explains how ATPase activity is turned off at night by a redox switch. Structures of mitochondrial ATP synthase dimers indicate how they shape the inner membrane cristae. The new cryo-EM structures complete our picture of the ATP synthases and reveal the unique mechanism by which they transform an electrochemical membrane potential into biologically useful chemical energy.

中文翻译：

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F型ATP合酶的结构和机制。

F1Fo ATP合酶在细胞中产生大部分ATP。对F型ATP合酶的研究已有50多年的历史，但只有通过电子冷冻显微镜（cryo-EM）确定的功能齐全的复合物的最新结构，才能全面了解其分子机制。高分辨率低温电磁结构提供了许多出乎意料的新见解。对于每个ATP产生功率冲程的第一部分，催化F1头随中心γ亚基一起旋转。关节旋转是通过充当F1和外围杆之间的柔性铰链的δ/ OSCP子单元实现的。亚单元a通过两个保守的水通道将质子传导到c环转子和从c环转子引出。通道在Fo的疏水核中被〜6Å隔开，导致产生强烈的局部磁场，从而产生扭矩来驱动F1中的旋转催化。叶绿体F1Fo复合物的结构解释了晚上如何通过氧化还原开关关闭ATPase活性。线粒体ATP合酶二聚体的结构表明它们如何塑造内膜cr。新的cryo-EM结构完善了我们对ATP合酶的描述，并揭示了它们将电化学膜电位转化为生物学上有用的化学能的独特机制。