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Proton Transport-Coupled ATP Synthesis Catalyzed by the Chloroplast ATPase

  • Peter Gräber
  • Ulrike Junesch
  • Günter Schmidt
  • Petra Fromme

Abstract

The membrane-bound ATPase in chloroplasts can catalyze ATP synthesis/hydrolysis coupled with a transmembrane proton transport. The detailed mechanism by which proton transport gives rise to the formation of a phosphate-anhydrid bond is still not known. We have investigated the kinetics of ATP synthesis with chloroplasts and with CFo F1 reconstituted into liposomes. From these results we want to draw conclusions about the mechanism of the reaction. The rate of ATP synthesis was measured with a rapid double-mixing system using artificially impressed transmembrane pH difference, ∆ pH, electric potential difference, ∆Ψ and phosphate potential, ∆Gp (1).

Keywords

Phosphate Potential Chemiosmotic Theory Electrochemical Potential Difference Chloroplast ATPase Centrifugation Column 
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

© Plenum Press, New York 1986

Authors and Affiliations

  • Peter Gräber
    • 1
  • Ulrike Junesch
    • 1
  • Günter Schmidt
    • 1
  • Petra Fromme
    • 1
  1. 1.Max-Volmer-Institut für Biophysikalische und Physikalische ChemieTechnische Universität BerlinBerlin 12Germany

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