Final answer:
Correct statements on the basic principles of the binding change mechanism of ATP synthase include the distinct interactions of the γ subunit with β-subunits, ATP binding affinities represented by L, T, and O conformations, and the production of three ATP molecules per full rotation of the γ subunit.
Step-by-step explanation:
The basic principles of the binding change mechanism concerning ATP synthase which accurately represent the process include:
- A. The γ subunit directly contacts all three β-subunits; however, each of these interactions is distinct, giving rise to three different β-subunit conformations.
- B. The ATP binding affinities of the three β-subunit conformations are L (loose), T (tight), and O (open). ADP and Pi bind to the L conformation, ATP binds tightly to the T conformation, and ATP is released from the enzyme when the β subunit is in the O conformation.
- C. As protons flow through Fo, the γ subunit rotates, facilitating a sequential conformational change in the β subunits from L to T to O to L with each 120° rotation.
Statement D is incorrect because one full rotation of the γ subunit generates three ATP molecules, not nine. For each 360° rotation, each β subunit cycles through L, T, and O states once, thereby coordinating the conformational states of all β subunits at a given time.