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

Research output: Contribution to journal › Article

23 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 languageEnglish
Pages (from-to)207-209
Number of pages3
JournalJournal of Bioenergetics and Biomembranes
Volume29
Issue number3
DOIs
Publication statusPublished - 1997
Externally publishedYes

Fingerprint

Proton-Translocating ATPases
Adenosine Triphosphate
Enzymes
Azides

Keywords

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

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme. / Yasuda, Ryohei; Noji, Hiroyuki; Kinosita, Kazuhiko; Motojima, Fumihiro; Yoshida, Masasuke.

In: Journal of Bioenergetics and Biomembranes, Vol. 29, No. 3, 1997, p. 207-209.

Research output: Contribution to journal › Article

Yasuda, R, Noji, H, Kinosita, K, Motojima, F & Yoshida, M 1997, 'Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme', Journal of Bioenergetics and Biomembranes, vol. 29, no. 3, pp. 207-209. https://doi.org/10.1023/A:1022449708449
Yasuda R, Noji H, Kinosita K, Motojima F, Yoshida M. Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme. Journal of Bioenergetics and Biomembranes. 1997;29(3):207-209. https://doi.org/10.1023/A:1022449708449
Yasuda, Ryohei ; Noji, Hiroyuki ; Kinosita, Kazuhiko ; Motojima, Fumihiro ; Yoshida, Masasuke. / Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme. In: Journal of Bioenergetics and Biomembranes. 1997 ; Vol. 29, No. 3. pp. 207-209.
@article{685de96e7a944700b105f2665ae8d277,
title = "Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme",
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.",
keywords = "ATP synthase, F-ATPase, Loose coupling, Rotary motor, Single molecule imaging",
author = "Ryohei Yasuda and Hiroyuki Noji and Kazuhiko Kinosita and Fumihiro Motojima and Masasuke Yoshida",
year = "1997",
doi = "10.1023/A:1022449708449",
language = "English",
volume = "29",
pages = "207--209",
journal = "Journal of Bioenergetics and Biomembranes",
issn = "0145-479X",
publisher = "Springer New York",
number = "3",

}

TY - JOUR

T1 - Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme

AU - Yasuda, Ryohei

AU - Noji, Hiroyuki

AU - Kinosita, Kazuhiko

AU - Motojima, Fumihiro

AU - Yoshida, Masasuke

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

KW - ATP synthase

KW - F-ATPase

KW - Loose coupling

KW - Rotary motor

KW - Single molecule imaging

UR - http://www.scopus.com/inward/record.url?scp=0030752655&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030752655&partnerID=8YFLogxK

U2 - 10.1023/A:1022449708449

DO - 10.1023/A:1022449708449

M3 - Article

C2 - 9298705

AN - SCOPUS:0030752655

VL - 29

SP - 207

EP - 209

JO - Journal of Bioenergetics and Biomembranes

JF - Journal of Bioenergetics and Biomembranes

SN - 0145-479X

IS - 3

ER -

Access to Document