Asymmetric enzyme kinetics of F1-ATPase resulted from asymmetric allosterism

Bio-molecular machines play various roles in cells where thermal fluctuation is dominant. Since artificial molecular machines are far behind bio-molecular machines for the present, we should begin with understanding how bio-molecular machines are designed to play their roles. We examine the motion of a bio-molecular machine, F1-ATPase, in single molecule experiments. In particular, we focus on the operation of F1-ATPase as ATP synthase in addition to as molecular motor. In this seminar, I talk about the enzyme kinetics, dependence of reaction rate on substrate concentration, of F1-ATPase in ATP synthesis. The experimental result shows that the enzyme kinetics of F1-ATPase in ATP synthesis exhibits weaker dependence on substrate concentration than the ordinary Michaelis-Menten kinetics, whereas that in ATP hydrolysis follows Michaelis-Menten kinetics. Therefore, the enzyme kinetics of F1-ATPase turned out to be asymmetric between ATP synthesis and hydrolysis. We analyzed this asymmetry based on a potential switching model, totally asymmetric allosteric model, whose characteristic is asymmetry in angular dependence of binding rates of substrates. It was shown that the totally asymmetric allosteric model may reproduce the experimental results, where the asymmetry of binding rates is essential. We also discuss physiological roles that the asymmetry of enzyme kinetics may play.