ATP Synthase: Structure and Mechanism

This lecture covers the structure and mechanism of ATP synthase, also known as Complex V, which generates ATP molecules using the proton motive force due to the H+ gradient. The structure consists of two major regions: FO and F1, with the F1 region being the catalytic subunit and the FO region being hydrophobic. The alpha and beta subunits form a hexametric hetero-oligomer responsible for binding ADP and Pi, catalyzing ATP synthesis, and releasing ATP. The rotation of the gamma subunit drives the interconversion of the beta subunit states, leading to ATP release through the binding-change mechanism. The movement of H+ through the a subunit powers the rotation of the c ring, causing the central stalk to rotate and stimulate ATP release.