Nucleotide Exchange Mechanism Involving Angle-Dependent Rate Constants Extracted from F1-ATPase Single-Molecule Rotation Trajectories.

ABSTRACT: Evidence has been mounting that in the rotational cycle of F1-ATPase there is a concerted ATP binding and ADP release that yields a million-fold acceleration in the rate of the product ADP release. We developed a theory of reaction kinetics to investigate the relationship between the concerted nucleotide exchange and previous single-molecule forced rotation data from Adachi, K. Nat. Commun. 2012, 3, 1022. We extracted from these data angle-dependent rate constants for nucleotide binding and release. The rate constants were then used in a unified kinetic scheme, also consistent with other single-molecule and ensemble experiments, to obtain analytical equations for nucleotide occupancy change events from nano- to millimolar ATP concentrations. A theory-experiment comparison revealed n

SUBMITTER: Volkan-Kacso S 

PROVIDER: S-EPMC12814531 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature