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Cited by 446

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F 0 F 1 ): Direct Observation

Sambongi, Yoshihiro, Iko, Yuko, Tanabe, Mikio, Omote, Hiroshi, Iwamoto-Kihara, Atsuko, Ueda, Ikuo, Yanagida, Toshio, Wada, Yoh, Futai, Masamitsu·1999·Science

Abstract

F 0 F 1 , found in mitochondria or bacterial membranes, synthesizes adenosine 5′-triphosphate (ATP) coupling with an electrochemical proton gradient and also reversibly hydrolyzes ATP to form the gradient. An actin filament connected to a c subunit oligomer of F 0 was able to rotate by using the energy of ATP hydrolysis. The rotary torque produced by the c subunit oligomer reached about 40 piconewton-nanometers, which is similar to that generated by the γ subunit in the F 1 motor. These results suggest that the γ and c subunits rotate together during ATP hydrolysis and synthesis. Thus, coupled rotation may be essential for energy coupling between proton transport through F 0 and ATP hydrolysis or synthesis in F 1 .

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Metadata

Authors
Sambongi, Y., Iko, Y., Tanabe, M., Omote, H., Iwamoto-Kihara, A., Ueda, I., Yanagida, T., Wada, Y., & Futai, M.
Venue
Science
Published
1999-11-26
Volume
286
Issue
5445
Pages
1722-1724
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2063339521
Cited by
446
References
1
FWCI
14.68
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F 0 F 1 ): Direct Observation. https://app.cochat.ai/papers/10.1126/science.286.5445.1722
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Sambongi, Y., Iko, Y., Tanabe, M., Omote, H., Iwamoto-Kihara, A., Ueda, I., Yanagida, T., Wada, Y., & Futai, M. (1999). Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F 0 F 1 ): Direct Observation. Science. https://doi.org/10.1126/science.286.5445.1722

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