KINETICS OF PROTON-TRANSPORT-COUPLED ATP SYNTHESIS CATALYZED BY THE CHLOROPLAST ATP SYNTHASE.

P. Graeber, Petra Fromme, U. Junesch, G. Schmidt, G. Thulke

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The kinetics of proton-transport-coupled ATP synthesis catalyzed by the chloroplast ATPase (ATP synthase) was investigated after energization of the membrane by an artificially generated DELTA pH and an electric potential difference, DELTA psi . With a rapid mixing system, ATP synthesis was studied at short reaction times ( less than 200 ms) where all relevant parameters (pH//o//u//t, pH//i//n, DELTA psi , substrate and product concentrations) remain practically constant at their initial values. The reaction is investigated at three levels of complexity. (1) The ATPase is embedded in the natural membrane. (2) The ATPase is isolated, purified and reconstituted into asolectin liposomes. (3) The reconstituted ATPase is investigated under single site, single turnover conditions.

Original languageEnglish
Pages (from-to)1034-1040
Number of pages7
JournalBerichte der Bunsengesellschaft/Physical Chemistry Chemical Physics
Volume11
Issue number90
Publication statusPublished - Nov 1986

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Chloroplast Proton-Translocating ATPases
Enzyme kinetics
Adenosinetriphosphate
Protons
Adenosine Triphosphate
Kinetics
Membranes
Liposomes
Electric potential
Substrates

ASJC Scopus subject areas

  • Chemical Engineering(all)

Cite this

KINETICS OF PROTON-TRANSPORT-COUPLED ATP SYNTHESIS CATALYZED BY THE CHLOROPLAST ATP SYNTHASE. / Graeber, P.; Fromme, Petra; Junesch, U.; Schmidt, G.; Thulke, G.

In: Berichte der Bunsengesellschaft/Physical Chemistry Chemical Physics, Vol. 11, No. 90, 11.1986, p. 1034-1040.

Research output: Contribution to journalArticle

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