Rotation of F₁-ATPase: The stochastic model

In this work, we consider a stochastic model describing the unidirectional rotation of the rotor (subunit γ) of F₁-ATPase. For appropriate choice of the model parameters, we used literature data on dynamic parameters of F₁-ATPase and results of our calculations of electrostatic interactions in enzyme-substrate complex of the catalytic cycle. The model takes into account thermal fluctuations of the bath and stochastic processes of substrate binding and product dissociation from the catalytic centers. The model provides an adequate description of ATP-driven rotations of subunit in F ₁-ATPase.