Theoretical analysis of the F(1)-ATPase experimental data.
F(1)-ATPase is a rotatory molecular motor fueled by ATP nucleotides. Different loads can be attached to the motor axis to show that it rotates in main discrete steps of 120 degrees with substeps of approximately 80 degrees and 40 degrees . Experimental data show the dependence on the mean rotational velocity omega with respect to the external control parameters: the nucleotide concentration [ATP] and the friction of the load gamma(L). In this work we present a theoretical analysis of the experimental data whose main results are: 1), A derivation of a simple analytical formula for omega([ATP], gamma(L)) that compares favorably with experiments; 2), The introduction of a two-state flashing ratchet model that exhibits experimental phenomenology of a greater specificity than has been, to our knowledge, previously available; 3), The derivation of an argument to obtain the values of the substep sizes; 4), An analysis of the energy constraints of the model; and 5), The theoretical analysis of the coupling ratio between the ATP consumed and the success of a forward step. We also discuss the compatibility of our approach with recent experimental observations.
Department of Estructura i Constituents de la Materia, Facultat de Fisica, Universitat de Barcelona, Barcelona, Spain. rperez@ecm.ub.es
Ruben
R
Perez-Carrasco
J M
JM
Sancho
D000255:Adenosine Triphosphate / Q000737:chemistry; D000465:Algorithms; D001419:Bacteria / Q000737:chemistry / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry; D003198:Computer Simulation; D004548:Elasticity; D017276:Friction; D008956:Models, Chemical; D009038:Motion; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D012399:Rotation; D013269:Stochastic Processes; D013696:Temperature; D013997:Time Factors
D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases