Mutational analysis of F1F0 ATPase

Catalysis and energy coupling

Hiroshi Omote, M. Futai

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Escherichia coli ATP synthase has eight subunits and functions through transmission of conformational changes between subunits. Extensive mutational analyses identified essential residues for catalysis and conformation transmission. Pseudorevertant studies revealed that β/α and β/γ subunits interactions are important for the energy coupling between catalysis and H+ translocation. In this article, we discuss mechanism of catalysis and energy coupling based on our recent mutation studies.

Original languageEnglish
Pages (from-to)177-183
Number of pages7
JournalActa Physiologica Scandinavica, Supplement
Volume163
Issue number643
Publication statusPublished - 1998
Externally publishedYes

Fingerprint

Catalysis
Adenosine Triphosphatases
Adenosine Triphosphate
Escherichia coli
Mutation

Keywords

  • ATP synthase
  • Mutagenesis
  • Pseudorevertant
  • Rotation
  • Rotational catalysis

ASJC Scopus subject areas

  • Physiology

Cite this

Mutational analysis of F1F0 ATPase : Catalysis and energy coupling. / Omote, Hiroshi; Futai, M.

In: Acta Physiologica Scandinavica, Supplement, Vol. 163, No. 643, 1998, p. 177-183.

Research output: Contribution to journalArticle

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