Nucleotide Exchange Mechanism Involving Angle-Dependent Rate Constants Extracted from F1-ATPase Single-Molecule Rotation Trajectories
Sándor Volkán-Kacsó, Ricardo A. Matute, Maria-Elisabeth Michel-Beyerle, Oganes Khatchikian, Rudolph A. Marcus
TL;DR
This paper studies how F1-ATPase rotates by analyzing nucleotide exchange rates, revealing a coordinated mechanism of ATP binding and ADP release.
Contribution
A new theory of reaction kinetics is developed to extract angle-dependent rate constants from single-molecule rotation data.
Findings
Angle-dependent rate constants for nucleotide binding and release were extracted from F1-ATPase rotation data.
The concerted mechanism is driven by correlated conformational changes in the F1-ATPase ring.
The kinetic signature is a unified function independent of ATP concentration.
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 AdachiK., Nat. Commun. 2012, 3, 1022 22929779 10.1038/ncomms2026PMC3449090. 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 novel evidence about the concerted mechanism: it is determined…
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Taxonomy
TopicsATP Synthase and ATPases Research · Bacterial Genetics and Biotechnology · Mitochondrial Function and Pathology