Letters to Nature

Nature 427, 465-468 (29 January 2004) | doi:10.1038/nature02212; Received 5 May 2003; Accepted 31 October 2003

Mechanically driven ATP synthesis by F1-ATPase

Hiroyasu Itoh1,2, Akira Takahashi3, Kengo Adachi4, Hiroyuki Noji5, Ryohei Yasuda6, Masasuke Yoshida7 & Kazuhiko Kinosita, Jr4

  1. Tsukuba Research Laboratory, Hamamatsu Photonics KK, Joko, Hamamatsu 431-3103, Japan
  2. CREST "Creation and application of soft nano-machine, the hyperfunctional molecular machine" Team 13*, Tokodai, Tsukuba 300-2635, Japan
  3. System Division, Hamamatsu Photonics KK, Joko, Hamamatsu 431-3103, Japan
  4. Center for Integrative Bioscience, Okazaki National Research Institutes, Okazaki 444-8585, Japan
  5. Institute of Industrial Science, University of Tokyo, Tokyo 153-8505, Japan
  6. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724 USA
  7. ERATO "ATP System", 5800-3 Nagatsuta, Yokohama 226-0026, Japan

Correspondence to: Hiroyasu Itoh1,2 Correspondence and requests for materials should be addressed to H.I. (Email: hiritoh@hpk.trc-net.co.jp).

ATP, the main biological energy currency, is synthesized from ADP and inorganic phosphate by ATP synthase in an energy-requiring reaction1, 2, 3. The F1 portion of ATP synthase, also known as F1-ATPase, functions as a rotary molecular motor: in vitro its gamma-subunit rotates4 against the surrounding alpha3beta3 subunits5, hydrolysing ATP in three separate catalytic sites on the beta-subunits. It is widely believed that reverse rotation of the gamma-subunit, driven by proton flow through the associated Fo portion of ATP synthase, leads to ATP synthesis in biological systems1, 2, 3, 6, 7. Here we present direct evidence for the chemical synthesis of ATP driven by mechanical energy. We attached a magnetic bead to the gamma-subunit of isolated F1 on a glass surface, and rotated the bead using electrical magnets. Rotation in the appropriate direction resulted in the appearance of ATP in the medium as detected by the luciferase–luciferin reaction. This shows that a vectorial force (torque) working at one particular point on a protein machine can influence a chemical reaction occurring in physically remote catalytic sites, driving the reaction far from equilibrium.

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