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 language | English |
|---|---|
| Pages (from-to) | 287-291 |
| Number of pages | 5 |
| Journal | European Journal of Biochemistry |
| Volume | 210 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1 Jan 1992 |
| MoE publication type | Not Eligible |
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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 journal › Article › Scientific › peer-review
TY - JOUR
T1 - Kinetics of ATP synthesis catalyzed by the H+‐ATPase from chloroplasts (CF0F1) reconstituted into liposomes and coreconstituted with bacteriorhodopsin
AU - Richard, Peter
AU - Gräber, Peter
PY - 1992/1/1
Y1 - 1992/1/1
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.
UR - http://www.scopus.com/inward/record.url?scp=0026470901&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1992.tb17419.x
DO - 10.1111/j.1432-1033.1992.tb17419.x
M3 - Article
C2 - 1446676
AN - SCOPUS:0026470901
VL - 210
SP - 287
EP - 291
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 1
ER -