Kinetics of ATP synthesis catalyzed by the H+‐ATPase from chloroplasts (CF0F1) reconstituted into liposomes and coreconstituted with bacteriorhodopsin

Peter Richard (Corresponding Author), Peter Gräber

Research output: Contribution to journalArticleScientificpeer-review

16 Citations (Scopus)

Abstract

The H+‐ATPase from chloroplasts (CF0F1) was isolated, purified and reconstituted into liposomes from phosphatidylcholine/phosphatidic acid. A transmembrane pH difference, pH, and a transmembrane electric potential difference, Ψ, were generate by an acid/base transition. The rate of ATP synthesis was measured at constant pH and constant Ψ as a function of temperature between 5°C and 45°C. The activation energy was 55 kJ mol−1. CF0F1 was coreconstituted with bacteriohodopsin at a molar ratio of approximately 1:170 in the same type of liposomes. Illumination of the proteoliposomes leads to proton transport into the vesicles generating a constant pH = 1.8. The dependence of the rate of ATP synthesis on ADP concentration was measured with CF0F1 in the oxidized state, Eox, and in the reduced state, Ered. The results can be described by Michaelis‐Menten kinetics with the following parameters: Vmax= 0.5 s−1, Km= 8 μLM for Eox and Vmax= 2.0 s−1, Km= 8 μLM for Ered.

Original languageEnglish
Pages (from-to)287-291
Number of pages5
JournalEuropean Journal of Biochemistry
Volume210
Issue number1
DOIs
Publication statusPublished - 1 Jan 1992
MoE publication typeNot Eligible

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Bacteriorhodopsins
Proton-Translocating ATPases
Chloroplasts
Liposomes
Adenosine Triphosphate
Phosphatidic Acids
Kinetics
Phosphatidylcholines
Adenosine Diphosphate
Protons
Activation energy
Lighting
Transport Vesicles
Acids
Electric potential
Membrane Potentials
Temperature
proteoliposomes

Cite this

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title = "Kinetics of ATP synthesis catalyzed by the H+‐ATPase from chloroplasts (CF0F1) reconstituted into liposomes and coreconstituted with bacteriorhodopsin",
abstract = "The H+‐ATPase from chloroplasts (CF0F1) was isolated, purified and reconstituted into liposomes from phosphatidylcholine/phosphatidic acid. A transmembrane pH difference, pH, and a transmembrane electric potential difference, Ψ, were generate by an acid/base transition. The rate of ATP synthesis was measured at constant pH and constant Ψ as a function of temperature between 5°C and 45°C. The activation energy was 55 kJ mol−1. CF0F1 was coreconstituted with bacteriohodopsin at a molar ratio of approximately 1:170 in the same type of liposomes. Illumination of the proteoliposomes leads to proton transport into the vesicles generating a constant pH = 1.8. The dependence of the rate of ATP synthesis on ADP concentration was measured with CF0F1 in the oxidized state, Eox, and in the reduced state, Ered. The results can be described by Michaelis‐Menten kinetics with the following parameters: Vmax= 0.5 s−1, Km= 8 μLM for Eox and Vmax= 2.0 s−1, Km= 8 μLM for Ered.",
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Kinetics of ATP synthesis catalyzed by the H+‐ATPase from chloroplasts (CF0F1) reconstituted into liposomes and coreconstituted with bacteriorhodopsin. / Richard, Peter (Corresponding Author); Gräber, Peter.

In: European Journal of Biochemistry, Vol. 210, No. 1, 01.01.1992, p. 287-291.

Research output: Contribution to journalArticleScientificpeer-review

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N2 - The H+‐ATPase from chloroplasts (CF0F1) was isolated, purified and reconstituted into liposomes from phosphatidylcholine/phosphatidic acid. A transmembrane pH difference, pH, and a transmembrane electric potential difference, Ψ, were generate by an acid/base transition. The rate of ATP synthesis was measured at constant pH and constant Ψ as a function of temperature between 5°C and 45°C. The activation energy was 55 kJ mol−1. CF0F1 was coreconstituted with bacteriohodopsin at a molar ratio of approximately 1:170 in the same type of liposomes. Illumination of the proteoliposomes leads to proton transport into the vesicles generating a constant pH = 1.8. The dependence of the rate of ATP synthesis on ADP concentration was measured with CF0F1 in the oxidized state, Eox, and in the reduced state, Ered. The results can be described by Michaelis‐Menten kinetics with the following parameters: Vmax= 0.5 s−1, Km= 8 μLM for Eox and Vmax= 2.0 s−1, Km= 8 μLM for Ered.

AB - The H+‐ATPase from chloroplasts (CF0F1) was isolated, purified and reconstituted into liposomes from phosphatidylcholine/phosphatidic acid. A transmembrane pH difference, pH, and a transmembrane electric potential difference, Ψ, were generate by an acid/base transition. The rate of ATP synthesis was measured at constant pH and constant Ψ as a function of temperature between 5°C and 45°C. The activation energy was 55 kJ mol−1. CF0F1 was coreconstituted with bacteriohodopsin at a molar ratio of approximately 1:170 in the same type of liposomes. Illumination of the proteoliposomes leads to proton transport into the vesicles generating a constant pH = 1.8. The dependence of the rate of ATP synthesis on ADP concentration was measured with CF0F1 in the oxidized state, Eox, and in the reduced state, Ered. The results can be described by Michaelis‐Menten kinetics with the following parameters: Vmax= 0.5 s−1, Km= 8 μLM for Eox and Vmax= 2.0 s−1, Km= 8 μLM for Ered.

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