What are the Mechanistic Insights of ATP Synthase Catalysis?
The catalysis by ATP Synthase involves several intermediate steps and complex conformational changes. The enzyme follows a binding change mechanism, where the rotation of the γ subunit within the F1 unit leads to different conformational states: open, loose, and tight. These states facilitate the binding of ADP and Pi, the synthesis of ATP, and the release of the newly formed ATP molecule.
