Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme

Ryohei Yasuda; Hiroyuki Noji; Kazuhiko Kinosita; Fumihiro Motojima; Masasuke Yoshida

doi:10.1023/A:1022449708449

Rotation of the γ subunit in F₁-ATPase; Evidence that ATP synthase is a rotary motor enzyme

Ryohei Yasuda, Hiroyuki Noji, Kazuhiko Kinosita, Fumihiro Motojima, Masasuke Yoshida^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

25 Citations (Scopus)

Abstract

ATP-dependent, azide-sensitive rotation of the γ subunit relative to the α₃β₃ hexagonal ring of ATP synthase was observed with a single molecule imaging system. Thus, ATP synthase is a rotary motor enzyme, the first ever found.

Original language	English
Pages (from-to)	207-209
Number of pages	3
Journal	Journal of Bioenergetics and Biomembranes
Volume	29
Issue number	3
DOIs	https://doi.org/10.1023/A:1022449708449
Publication status	Published - 1997
Externally published	Yes

Keywords

ATP synthase
F-ATPase
Loose coupling
Rotary motor
Single molecule imaging

ASJC Scopus subject areas

Physiology
Cell Biology

Access to Document

10.1023/A:1022449708449

Cite this

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abstract = "ATP-dependent, azide-sensitive rotation of the γ subunit relative to the α3β3 hexagonal ring of ATP synthase was observed with a single molecule imaging system. Thus, ATP synthase is a rotary motor enzyme, the first ever found.",

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author = "Ryohei Yasuda and Hiroyuki Noji and Kazuhiko Kinosita and Fumihiro Motojima and Masasuke Yoshida",

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AU - Noji, Hiroyuki

AU - Kinosita, Kazuhiko

AU - Motojima, Fumihiro

AU - Yoshida, Masasuke

PY - 1997

Y1 - 1997

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KW - F-ATPase

KW - Loose coupling

KW - Rotary motor

KW - Single molecule imaging

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