F-type H+-ATPase: Catalysis and Proton Transport

  • Atsuko Iwamoto
  • Hiroshi Omote
  • Robert K. Nakamoto
  • Masatomo Maeda
  • Masamitsu Futai
Conference paper
Part of the NATO ASI Series book series (NATO ASI, volume 89)


F0F1 H+ATPase (or F-type ATPase) catalyzes ATP synthesis or hydrolysis coupling with proton translocation (for reviews, see Futai et al., 1989; Senior, 1990; Fillingame, 1990). The F-type ATPase of Escherichia coli is similar to those found in inner mitochondrial or chloroplast thylakoid membranes, and has contributed greatly to the understanding of this complicated enzyme. The catalytic site of the enzyme is in the P subunit or at the interface between the α and β subunits of the membrane extrinsic F1 sector. The proton pathway is formed from the a, b, and c subunits of the membrane intrinsic Fo sector. The γ, δ, and ε subunits of F1 are required functionally and structurally to connect the catalytic subunits to the Fo sector. The mechanism of ATP hydrolysis can be studied using purified F1 (F1 — ATPase).


Catalytic Site Mutant Enzyme Energy Coupling Proton Translocation Phosphate Moiety 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer-Verlag Berlin Heidelberg 1994

Authors and Affiliations

  • Atsuko Iwamoto
    • 1
  • Hiroshi Omote
    • 1
  • Robert K. Nakamoto
    • 1
  • Masatomo Maeda
    • 1
  • Masamitsu Futai
    • 1
  1. 1.Department of Organic Chemistry and Biochemistry Institute of Scientific and Industrial ResearchOsaka UniversityIbaraki, OsakaJapan

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