F 1-ATPase: A highly efficient rotary ATP machine

Kazuhiko Kinosita, Ryohei Yasuda, Hiroyuki Noji

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

• A single molecule of F 1-ATPase is by itself a rotary motor in which a central subunit, γ, rotates against a surrounding stator cylinder made of α 3β 3 hexamer. • Driven by the three β subunits that hydrolyse ATP sequentially, the motor runs with discrete 120° steps at low ATP concentrations. • Over broad ranges of load and speed, the motor produces a constant torque of 40 pN·nm. • The mechanical work the motor does in the 120° step, or the work per ATP hydrolysed, is also constant and amounts to 80-90 pN·nm, which is close to the free energy of ATP hydrolysis. Thus this motor can work at near 100% efficiency.

Original languageEnglish
Pages (from-to)3-18
Number of pages16
JournalEssays in Biochemistry
Volume35
Publication statusPublished - 2000
Externally publishedYes

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Proton-Translocating ATPases
Adenosine Triphosphate
Torque
Hydrolysis
Stators
Free energy
Loads (forces)
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinosita, K., Yasuda, R., & Noji, H. (2000). F 1-ATPase: A highly efficient rotary ATP machine. Essays in Biochemistry, 35, 3-18.

F 1-ATPase : A highly efficient rotary ATP machine. / Kinosita, Kazuhiko; Yasuda, Ryohei; Noji, Hiroyuki.

In: Essays in Biochemistry, Vol. 35, 2000, p. 3-18.

Research output: Contribution to journalArticle

Kinosita, K, Yasuda, R & Noji, H 2000, 'F 1-ATPase: A highly efficient rotary ATP machine', Essays in Biochemistry, vol. 35, pp. 3-18.
Kinosita, Kazuhiko ; Yasuda, Ryohei ; Noji, Hiroyuki. / F 1-ATPase : A highly efficient rotary ATP machine. In: Essays in Biochemistry. 2000 ; Vol. 35. pp. 3-18.
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