Nonequilibrium energetics of a single F1-ATPase molecule

Details Nonequilibrium energetics of a single F1-ATPase molecule Nonequilibrium energetics of a single F1-ATPase molecule

2010-02-09

arxiv.org/abs/1002.1867v1

Phys. Rev. Lett. 104, 198103 (2010)

Physics

Condensed Matter

Statistical Mechanics

4 pages, 4 figures

Scientific paper

10.1103/PhysRevLett.104.198103

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.

Affiliated with

Also associated with

No associations

Rating

Nonequilibrium energetics of a single F1-ATPase molecule does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Nonequilibrium energetics of a single F1-ATPase molecule, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Nonequilibrium energetics of a single F1-ATPase molecule will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-124718