Mechanically driven ATP synthesis by F1-ATPase

Hiroyasu Itoh, Akira Takahashi, Kengo Adachi, Hiroyuki Noji, Ryohei Yasuda, Masasuke Yoshida, Kazuhiko Kinosita

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406 Citations (Scopus)

Abstract

ATP, the main biological energy currency, is synthesized from ADP and inorganic phosphate by ATP synthase in an energy-requiring reaction. The F 1 portion of ATP synthase, also known as F1-ATPase, functions as a rotary molecular motor: in vitro its γ-subunit rotates against the surrounding α3β3 subunits, hydrolysing ATP in three separate catalytic sites on the β-subunits. It is widely believed that reverse rotation of the γ-subunit, driven by proton flow through the associated Fo portion of ATP synthase, leads to ATP synthesis in biological systems. Here we present direct evidence for the chemical synthesis of ATP driven by mechanical energy. We attached a magnetic bead to the γ-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.

Original languageEnglish
Pages (from-to)465-468
Number of pages4
JournalNature
Volume427
Issue number6973
DOIs
Publication statusPublished - 2004 Jan 29
Externally publishedYes

ASJC Scopus subject areas

  • General

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    Itoh, H., Takahashi, A., Adachi, K., Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (2004). Mechanically driven ATP synthesis by F1-ATPase. Nature, 427(6973), 465-468. https://doi.org/10.1038/nature02212