Conformational transmission in ATP synthase during catalysis: Search for large structural changes

Masamitsu Futai, Hiroshi Omote

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Escherichia coli ATP synthase has eight subunits and functions through transmission of conformational changes between subunits. Defective mutation at βGly-149 was suppressed by the second mutations at the outer surface of the β subunit, indicating that the defect by the first mutation was suppressed by the second mutation through long range conformation transmission. Extensive mutant/pseudorevertant studies revealed that β/α and β/γ subunits interactions are important for the energy coupling between catalysis and H+ translocation. In addition, long range interaction between amino and carboxyl terminal regions of the γ subunit has a critical role(s) for energy coupling. These results suggest that the dynamic conformation change and its transmission are essential for ATP synthase.

Original languageEnglish
Pages (from-to)409-414
Number of pages6
JournalJournal of Bioenergetics and Biomembranes
Volume28
Issue number5
Publication statusPublished - 1996
Externally publishedYes

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Catalysis
Adenosine Triphosphate
Mutation
Escherichia coli

Keywords

  • ATP synthase
  • conformation transmission
  • mutagenesis
  • pseudorevertant
  • rotational catalysis

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Conformational transmission in ATP synthase during catalysis : Search for large structural changes. / Futai, Masamitsu; Omote, Hiroshi.

In: Journal of Bioenergetics and Biomembranes, Vol. 28, No. 5, 1996, p. 409-414.

Research output: Contribution to journalArticle

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