Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation

Takayuki Nishizaka, Kazuhiro Oiwa, Hiroyuki Noji, Shigeki Kimura, Eiro Muneyuki, Masasuke Yoshida, Kazuhiko Kinosita

Research output: Contribution to journalArticle

217 Citations (Scopus)

Abstract

F1-ATPase is a rotary molecular motor in which unidirectional rotation of the central γ subunit is powered by ATP hydrolysis in three catalytic sites arranged 120° apart around γ. To study how hydrolysis reactions produce mechanical rotation, we observed rotation under an optical microscope to see which of the three sites bound and released a fluorescent ATP analog. Assuming that the analog mimics authentic ATP, the following scheme emerges: (i) in the ATP-waiting state, one site, dictated by the orientation of γ, is empty, whereas the other two bind a nucleotide; (ii) ATP binding to the empty site drives an ∼80° rotation of γ; (iii) this triggers a reaction(s), hydrolysis and/or phosphate release, but not ADP release in the site that bound ATP one step earlier; (iv) completion of this reaction induces further ∼40° rotation.

Original languageEnglish
Pages (from-to)142-148
Number of pages7
JournalNature Structural and Molecular Biology
Volume11
Issue number2
DOIs
Publication statusPublished - 2004 Feb
Externally publishedYes

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Proton-Translocating ATPases
Nucleotides
Adenosine Triphosphate
Observation
Hydrolysis
Optical Rotation
Adenosine Diphosphate
Catalytic Domain
Phosphates

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation. / Nishizaka, Takayuki; Oiwa, Kazuhiro; Noji, Hiroyuki; Kimura, Shigeki; Muneyuki, Eiro; Yoshida, Masasuke; Kinosita, Kazuhiko.

In: Nature Structural and Molecular Biology, Vol. 11, No. 2, 02.2004, p. 142-148.

Research output: Contribution to journalArticle

Nishizaka, T, Oiwa, K, Noji, H, Kimura, S, Muneyuki, E, Yoshida, M & Kinosita, K 2004, 'Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation', Nature Structural and Molecular Biology, vol. 11, no. 2, pp. 142-148. https://doi.org/10.1038/nsmb721
Nishizaka, Takayuki ; Oiwa, Kazuhiro ; Noji, Hiroyuki ; Kimura, Shigeki ; Muneyuki, Eiro ; Yoshida, Masasuke ; Kinosita, Kazuhiko. / Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation. In: Nature Structural and Molecular Biology. 2004 ; Vol. 11, No. 2. pp. 142-148.
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