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

P. Graeber; P. Fromme; U. Junesch; G. Schmidt; G. Thulke

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

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

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	1034-1040
Number of pages	7
Journal	Berichte der Bunsengesellschaft/Physical Chemistry Chemical Physics
Volume	11
Issue number	90
State	Published - Nov 1 1986
Externally published	Yes

ASJC Scopus subject areas

General Chemical Engineering

Cite this

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title = "KINETICS OF PROTON-TRANSPORT-COUPLED ATP SYNTHESIS CATALYZED BY THE CHLOROPLAST ATP SYNTHASE.",

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.",

author = "P. Graeber and P. Fromme and U. Junesch and G. Schmidt and G. Thulke",

year = "1986",

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AU - Graeber, P.

AU - Fromme, P.

AU - Junesch, U.

AU - Schmidt, G.

AU - Thulke, G.

PY - 1986/11/1

Y1 - 1986/11/1

N2 - 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.

AB - 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.

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

Abstract

ASJC Scopus subject areas

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