Systematic kinetics study of F₀F₁-ATPase: Analytic results and comparison with experiments

The systematic kinetics of the holoenzyme F₀F₁-ATPase has been investigated by a tri-site filled, random binding order, and stochastic mechanochemical tight coupling model. The connection between the mechanical rotation speed and the chemical quantities such as the concentrations of substrates, the proton motive force, and the mechanical damping coefficient, has been analytically derived. The enzymatics based on ensemble experiments and single-molecule assays can be discussed systematically. Our model predictions agree well with both ensemble and single-molecule experimental results. Furthermore, this model can be used to study the dynamics of F₀F ₁-ATPase in a vesicle system.