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Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
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| Personen und Körperschaften: | , , , |
| In: | Proceedings of the National Academy of Sciences, 109, 2012, 28, S. 11150-11155 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Petersen, Jan Förster, Kathrin Turina, Paola Gräber, Peter Petersen, Jan Förster, Kathrin Turina, Paola Gräber, Peter |
|---|---|
| author |
Petersen, Jan Förster, Kathrin Turina, Paola Gräber, Peter |
| spellingShingle |
Petersen, Jan Förster, Kathrin Turina, Paola Gräber, Peter Proceedings of the National Academy of Sciences Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast Multidisciplinary |
| author_sort |
petersen, jan |
| spelling |
Petersen, Jan Förster, Kathrin Turina, Paola Gräber, Peter 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1202799109 <jats:p> F <jats:sub>0</jats:sub> F <jats:sub>1</jats:sub> -ATP synthases use the free energy derived from a transmembrane proton transport to synthesize ATP from ADP and inorganic phosphate. The number of protons translocated per ATP (H <jats:sup>+</jats:sup> /ATP ratio) is an important parameter for the mechanism of the enzyme and for energy transduction in cells. Current models of rotational catalysis predict that the H <jats:sup>+</jats:sup> /ATP ratio is identical to the stoichiometric ratio of c-subunits to β-subunits. We measured in parallel the H <jats:sup>+</jats:sup> /ATP ratios at equilibrium of purified F <jats:sub>0</jats:sub> F <jats:sub>1</jats:sub> s from yeast mitochondria (c/β = 3.3) and from spinach chloroplasts (c/β = 4.7). The isolated enzymes were reconstituted into liposomes and, after energization of the proteoliposomes with acid–base transitions, the initial rates of ATP synthesis and hydrolysis were measured as a function of ΔpH. The equilibrium ΔpH was obtained by interpolation, and from its dependency on the stoichiometric ratio, [ATP]/([ADP]·[P <jats:sub>i</jats:sub> ]), finally the thermodynamic H <jats:sup>+</jats:sup> /ATP ratios were obtained: 2.9 ± 0.2 for the mitochondrial enzyme and 3.9 ± 0.3 for the chloroplast enzyme. The data show that the thermodynamic H <jats:sup>+</jats:sup> /ATP ratio depends on the stoichiometry of the c-subunit, although it is not identical to the c/β ratio. </jats:p> Comparison of the H <sup>+</sup> /ATP ratios of the H <sup>+</sup> -ATP synthases from yeast and from chloroplast Proceedings of the National Academy of Sciences |
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| title |
Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_unstemmed |
Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_full |
Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_fullStr |
Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_full_unstemmed |
Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_short |
Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_sort |
comparison of the h
<sup>+</sup>
/atp ratios of the h
<sup>+</sup>
-atp synthases from yeast and from chloroplast |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.1202799109 |
| publishDate |
2012 |
| physical |
11150-11155 |
| description |
<jats:p>
F
<jats:sub>0</jats:sub>
F
<jats:sub>1</jats:sub>
-ATP synthases use the free energy derived from a transmembrane proton transport to synthesize ATP from ADP and inorganic phosphate. The number of protons translocated per ATP (H
<jats:sup>+</jats:sup>
/ATP ratio) is an important parameter for the mechanism of the enzyme and for energy transduction in cells. Current models of rotational catalysis predict that the H
<jats:sup>+</jats:sup>
/ATP ratio is identical to the stoichiometric ratio of c-subunits to β-subunits. We measured in parallel the H
<jats:sup>+</jats:sup>
/ATP ratios at equilibrium of purified F
<jats:sub>0</jats:sub>
F
<jats:sub>1</jats:sub>
s from yeast mitochondria (c/β = 3.3) and from spinach chloroplasts (c/β = 4.7). The isolated enzymes were reconstituted into liposomes and, after energization of the proteoliposomes with acid–base transitions, the initial rates of ATP synthesis and hydrolysis were measured as a function of ΔpH. The equilibrium ΔpH was obtained by interpolation, and from its dependency on the stoichiometric ratio, [ATP]/([ADP]·[P
<jats:sub>i</jats:sub>
]), finally the thermodynamic H
<jats:sup>+</jats:sup>
/ATP ratios were obtained: 2.9 ± 0.2 for the mitochondrial enzyme and 3.9 ± 0.3 for the chloroplast enzyme. The data show that the thermodynamic H
<jats:sup>+</jats:sup>
/ATP ratio depends on the stoichiometry of the c-subunit, although it is not identical to the c/β ratio.
</jats:p> |
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| author | Petersen, Jan, Förster, Kathrin, Turina, Paola, Gräber, Peter |
| author_facet | Petersen, Jan, Förster, Kathrin, Turina, Paola, Gräber, Peter, Petersen, Jan, Förster, Kathrin, Turina, Paola, Gräber, Peter |
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| description | <jats:p> F <jats:sub>0</jats:sub> F <jats:sub>1</jats:sub> -ATP synthases use the free energy derived from a transmembrane proton transport to synthesize ATP from ADP and inorganic phosphate. The number of protons translocated per ATP (H <jats:sup>+</jats:sup> /ATP ratio) is an important parameter for the mechanism of the enzyme and for energy transduction in cells. Current models of rotational catalysis predict that the H <jats:sup>+</jats:sup> /ATP ratio is identical to the stoichiometric ratio of c-subunits to β-subunits. We measured in parallel the H <jats:sup>+</jats:sup> /ATP ratios at equilibrium of purified F <jats:sub>0</jats:sub> F <jats:sub>1</jats:sub> s from yeast mitochondria (c/β = 3.3) and from spinach chloroplasts (c/β = 4.7). The isolated enzymes were reconstituted into liposomes and, after energization of the proteoliposomes with acid–base transitions, the initial rates of ATP synthesis and hydrolysis were measured as a function of ΔpH. The equilibrium ΔpH was obtained by interpolation, and from its dependency on the stoichiometric ratio, [ATP]/([ADP]·[P <jats:sub>i</jats:sub> ]), finally the thermodynamic H <jats:sup>+</jats:sup> /ATP ratios were obtained: 2.9 ± 0.2 for the mitochondrial enzyme and 3.9 ± 0.3 for the chloroplast enzyme. The data show that the thermodynamic H <jats:sup>+</jats:sup> /ATP ratio depends on the stoichiometry of the c-subunit, although it is not identical to the c/β ratio. </jats:p> |
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| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1 |
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| spelling | Petersen, Jan Förster, Kathrin Turina, Paola Gräber, Peter 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1202799109 <jats:p> F <jats:sub>0</jats:sub> F <jats:sub>1</jats:sub> -ATP synthases use the free energy derived from a transmembrane proton transport to synthesize ATP from ADP and inorganic phosphate. The number of protons translocated per ATP (H <jats:sup>+</jats:sup> /ATP ratio) is an important parameter for the mechanism of the enzyme and for energy transduction in cells. Current models of rotational catalysis predict that the H <jats:sup>+</jats:sup> /ATP ratio is identical to the stoichiometric ratio of c-subunits to β-subunits. We measured in parallel the H <jats:sup>+</jats:sup> /ATP ratios at equilibrium of purified F <jats:sub>0</jats:sub> F <jats:sub>1</jats:sub> s from yeast mitochondria (c/β = 3.3) and from spinach chloroplasts (c/β = 4.7). The isolated enzymes were reconstituted into liposomes and, after energization of the proteoliposomes with acid–base transitions, the initial rates of ATP synthesis and hydrolysis were measured as a function of ΔpH. The equilibrium ΔpH was obtained by interpolation, and from its dependency on the stoichiometric ratio, [ATP]/([ADP]·[P <jats:sub>i</jats:sub> ]), finally the thermodynamic H <jats:sup>+</jats:sup> /ATP ratios were obtained: 2.9 ± 0.2 for the mitochondrial enzyme and 3.9 ± 0.3 for the chloroplast enzyme. The data show that the thermodynamic H <jats:sup>+</jats:sup> /ATP ratio depends on the stoichiometry of the c-subunit, although it is not identical to the c/β ratio. </jats:p> Comparison of the H <sup>+</sup> /ATP ratios of the H <sup>+</sup> -ATP synthases from yeast and from chloroplast Proceedings of the National Academy of Sciences |
| spellingShingle | Petersen, Jan, Förster, Kathrin, Turina, Paola, Gräber, Peter, Proceedings of the National Academy of Sciences, Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast, Multidisciplinary |
| title | Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_full | Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_fullStr | Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_full_unstemmed | Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_short | Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| title_sort | comparison of the h <sup>+</sup> /atp ratios of the h <sup>+</sup> -atp synthases from yeast and from chloroplast |
| title_unstemmed | Comparison of the H + /ATP ratios of the H + -ATP synthases from yeast and from chloroplast |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1202799109 |