One exchanges protons with IMS or outside the cell, and the other shuttles protons between the matrix and cytoplasm. The a-subunit possesses two half-channels. The F O motor harbors a ring-shaped c-subunit oligomer, which serves as the rotor, and an a-subunit (stator), which mediates proton transfer between the c-ring and outer membrane aqueous environment. Hybrid Monte Carlo and MD simulations showed how proton transfer is coupled to rotation.į OF 1 ATP synthase, a ubiquitous enzyme that synthesizes most ATP in living cells, comprises two rotary motors: the membrane-embedded proton-driven F O motor and the catalytic F 1 motor these motors share the central rotor and peripheral stalk.
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Coarse-grained MD simulations unveiled a free energy surface based on the protonation state and rotational angle of the rotor. All-atom molecular dynamics (MD) simulations elucidated changes in the protonation/deprotonation of glutamate-the protein-carrier residue-during rotation and revealed the protonation states that form the “water wire” required for long-range proton hopping. Here, we review theoretical and computational studies based on F O structure models. Despite high resolution, however, static information alone cannot elucidate how and where the protons pass through the F O and how proton passage is coupled to F O rotation.
Recently, many near-atomic resolution structural models have been obtained using cryo-electron microscopy. In F OF 1 ATP synthase, driven by the proton motive force across the membrane, the F O motor rotates the central rotor and induces conformational changes in the F 1 motor, resulting in ATP synthesis.
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