Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F 1 -ATPase
Abstract
The investigation of nucleotide binding and release dynamics vs. rotor shaft rotation in the F 1 -ATPase enzyme is necessary to reveal biological function. We elucidate the mechanism of the exponential-like change of binding and release rate (and thus the equilibrium) constants when probed against the rotor angle at the single-molecule level. We extend our group transfer theory proposed for the stalling experiments to treat controlled rotation experiments. The model correctly predicts the controlled rotation data on fluorescent ATP without any adjustable parameters. The theory provides a framework able to treat the binding and release of various nucleotides. In the process we also learn about the properties of the fluorescent nucleotide Cy3-ATP.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Oct 10, 2016
- Source ID
- 10.1073/pnas.1611601113
Entities
People
- Rudolph A. Marcus
- Sándor Volkán-kacsó
Organizations
- Army Research Office
- California Institute of Technology
- Office of Naval Research Global