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

Autori
Dewar, Roderick ; Juretić, Davor ; Županović, Paško

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
4th International Meeting on Maximum Entropy Production in Physics and Biology / Županović, Paško - Split : Fizikalno društvo, Split, 2006

Skup
4th International Meeting on Maximum Entropy Production in Physics and Biology

Mjesto i datum
Split, Hrvatska, 06.07.2006. - 07.07.2006

Vrsta sudjelovanja
Pozvano predavanje

Vrsta recenzije
Nije recenziran

Ključne riječi
ATP synthase; entropy production

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Biologija

POVEZANOST RADA