Nonequilibrium energetics of a single F1-ATPase molecule
Abstract
Molecular motors drive mechanical motions utilizing the free energy liberated from chemical reactions such as ATP hydrolysis. Although it is essential to know the efficiency of this free energy transduction, it has been a challenge due to the system's microscopic scale. Here, we evaluate the single-molecule energetics of a rotary molecular motor, F1-ATPase, by applying a recently derived nonequilibrium equality together with an electrorotation method. We show that the sum of the heat flow through the probe's rotational degree of freedom and the work against external load is almost equal to the free energy change per a single ATP hydrolysis under various conditions. This implies that F1-ATPase works at an efficiency of nearly 100% in a thermally fluctuating environment.
Keywords
Cite
@article{arxiv.1002.1867,
title = {Nonequilibrium energetics of a single F1-ATPase molecule},
author = {Shoichi Toyabe and Tetsuaki Okamoto and Takahiro Watanabe-Nakayama and Hiroshi Taketani and Seishi Kudo and Eiro Muneyuki},
journal= {arXiv preprint arXiv:1002.1867},
year = {2017}
}
Comments
4 pages, 4 figures