Theory for rates, equilibrium constants, and Brønsted slopes in F 1 -ATPase single molecule imaging experiments
Abstract
The biological function in the F1-ATPase enzyme can be elucidated by understanding the dynamical interplay of reactions and mechanical rotation in the protein. Recent single molecule imaging and rotor manipulation experiments revealed that the rate constants of enzymatic steps, such as ATP binding or phosphate release, show an exponential dependence on the stalled rotor angle. Following concepts that originated in theories of electron and group transfer reactions, a structure-based analytic model is described to treat the dynamical behavior observed in these experiments. Using biochemical and the single molecule observations, thermodynamic driving potentials are constructed that take into account the elasticity of the rotor shaft. The model predicts observable quantities without using adjustable parameters and is tested using existing data.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Oct 19, 2015
- Source ID
- 10.1073/pnas.1518489112
Entities
People
- Rudolph A. Marcus
- Sándor Volkán-kacsó
Organizations
- Army Research Office
- California Institute of Technology