Rotation of F1-ATPase: How an ATP-Driven Molecular Machine May Work

Author:

Kinosita Kazuhiko1,Adachi Kengo1,Itoh Hiroyasu23

Affiliation:

1. Center for Integrative Bioscience, Okazaki National Research Institutes, Higashiyama 5-1, Myodaiji, Okazaki 444-8585, Japan;

2. Tsukuba Research Laboratory, Hamamatsu Photonics KK, Tokodai, Tsukuba 300-2635, Japan

3. CREST “Creation and Application of Soft Nano-Machine, the Hyperfunctional Molecular Machine” Team 13*, Tokodai, Tsukuba 300-2635, Japan;

Abstract

▪ Abstract  F1-ATPase is a rotary motor made of a single protein molecule. Its rotation is driven by free energy obtained by ATP hydrolysis. In vivo, another motor, Fo, presumably rotates the F1 motor in the reverse direction, reversing also the chemical reaction in F1 to let it synthesize ATP. Here we attempt to answer two related questions, How is free energy obtained by ATP hydrolysis converted to the mechanical work of rotation, and how is mechanical work done on F1 converted to free energy to produce ATP? After summarizing single-molecule observations of F1 rotation, we introduce a toy model and discuss its free-energy diagrams to possibly answer the above questions. We also discuss the efficiency of molecular motors in general.

Publisher

Annual Reviews

Subject

Structural Biology,Biophysics

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