title: A model of stepping kinetics for rotary enzymes. Application to the F1-ATPase.
abstract: Our simple kinetic model, based on the classic "binding change mechanism", describes the stepping kinetics for the rotary enzyme motors. The model shows that the cooperative interactions between active sites in the motor enzyme F1-ATPase induce the stepping product release. This phenomenon results from non-harmonic oscillations in the enzyme forms. The found rate constants, corresponding to the stepping phenomenon, are close to the rate constants known for the F1-ATPase. The duration of dwells during the product release is shown to depend on the ATP concentration in accordance with the known experimental data.
authors.affiliation: Institute of Theoretical and Experimental Biophysics Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia. goldstein.boris@yandex.ru
authors.forename: B N
authors.initials: BN
authors.lastname: Goldstein
authors.forename: A M
authors.initials: AM
authors.lastname: Aksirov
authors.forename: D T
authors.initials: DT
authors.lastname: Zakrjevskaya
mesh_terms: D000244:Adenosine Diphosphate / Q000737:chemistry / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006868:Hydrolysis; D007700:Kinetics; D008954:Models, Biological; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012399:Rotation
chemical_list: D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases