Simple Mechanical Equivalents of Stepping Rotary Dynamics in F$_1$-ATPase

摘要

Two simple (rotator and one-particle) mechanistic models are suggested todescribe simultaneously at a minimal level of sophistication two basicfunctions of F$_1$-ATPase: a motor regime driven by ATP hydrolysis and itsinverted function as ATP synthesis. This description is consistent with theso-called rotary binding-change mechanism, a milestone of functioning ATPsynthase, and uses a stepping (driving) function associated with two sequencesof time instants, at which hydrolysis and synthesis reactions occur. It isuseful to analyse experimental data and numerical simulations indeed predictcorresponding dynamic behavior.