The γ-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli

Hiroshi Omote, Noriko Sambonmatsu, Kiwamu Saito, Yoshihiro Sambongi, Atsuko Iwamoto-Kihara, Toshio Yanagida, Yoh Wada, Masamitsu Futai

Research output: Contribution to journalArticlepeer-review

119 Citations (Scopus)


The rotation of the γ-subunit has been included in the binding-change mechanism of ATP synthesis/ hydrolysis by the proton ATP synthase (FOF1). The Escherichia coli ATP synthase was engineered for rotation studies such that its ATP hydrolysis and synthesis activity is similar to that of wild type. A fluorescently labeled actin filament connected to the γ-subunit of the F1 sector rotated on addition of ATP. This progress enabled us to analyze the γM23K (the γ-subunit Met-23 replaced by Lys) mutant, which is defective in energy coupling between catalysis and proton translocation. We found that the F1 sector produced essentially the same frictional torque, regardless of the mutation. These results suggest that the γM23K mutant is defective in the transformation of the mechanical work into proton translocation or vice versa.

Original languageEnglish
Pages (from-to)7780-7784
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number14
Publication statusPublished - Jul 6 1999
Externally publishedYes


  • ATP synthase
  • Frictional torque
  • Rotational catalysis

ASJC Scopus subject areas

  • General


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