Mechanically driven ATP synthesis by F1-ATPase

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

*この研究の対応する著者

研究成果: Article査読

430 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)465-468
ページ数4
ジャーナルNature
427
6973
DOI
出版ステータスPublished - 2004 1月 29
外部発表はい

ASJC Scopus subject areas

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