engleski

Kinetic design of the rotary enzyme ATP synthase is consistent with maximal entropy production principle

Are living entities optimized to produce as little or as much entropy as possible? We show here that at least one important molecular motor – the ATP synthase – evolved in accord with the statistical selection principle of Maximum Shannon Entropy (MaxEnt) and one of its corrolaries – Maximum Entropy Production (MEP). By using these connected variational principles we derived the optimal values of the relative angular position of the ATP-binding transition, which is in accord with the experimental best-fit angular position. MaxEnt and MEP predict an inverse relationship between the ATP synthase gearing ratio and the proton motive force in the region of approximate linearity of flux-force relationship far from equilibrium (the inflection point). For such proton-motive force molecular motor reacts with the highest speed to produce additional ATP or to save ATP molecules.

ATP synthase; entropy production

nije evidentirano