ArticleProceedings of the National Academy of Sciences of the United States of America2008
The thermodynamic H+/ATP ratios of the H+-ATPsynthases from chloroplasts and Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 124 citations in OpenAlex.
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- Evaluation of Thiobacillus denitrificans' sustainability in nitrate-reducing Fe(II) oxidation and the potential significance of Fe(II) as a growth-supporting reductant.FEMS microbiology ecology · 2025Article
- The Warburg Effect is the result of faster ATP production by glycolysis than respiration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanism of ADP-Inhibited ATP Hydrolysis in Single Proton-Pumping FInternational journal of molecular sciences · 2023Article
- The multiple facets of mitochondrial regulations controlling cellular thermogenesis.Cellular and molecular life sciences : CMLS · 2022Review
- Laboratory evolution of synthetic electron transport system variants reveals a larger metabolic respiratory system and its plasticity.Nature communications · 2022Article
- Empowering roots-Some current aspects of root bioenergetics.Frontiers in plant science · 2022Review
- pH-dependent 11° FeLife · 2021Article
- Proton motive force in plant photosynthesis dominated by ΔpH in both low and high light.Plant physiology · 2021Article
- Evolution of a biochemical model of steady-state photosynthesis.Plant, cell & environment · 2021Review
- Catalytic Reactions and Energy Conservation in the CytochromeChemical reviews · 2021Review
- Recording and Simulating Proton-Related Metabolism in Bacterial Cell Suspensions.Frontiers in microbiology · 2021Article
- Microbial Upgrading of Acetate into Value-Added Products-Examining Microbial Diversity, Bioenergetic Constraints and Metabolic Engineering Approaches.International journal of molecular sciences · 2020Review
- Optimization of ATP Synthase c-Rings for Oxygenic Photosynthesis.Frontiers in plant science · 2019Article
- The energy budget in CThe New phytologist · 2018Article
- In Silico Analysis of the Regulation of the Photosynthetic Electron Transport Chain in C3 Plants.Plant physiology · 2018Article
- Deleting the IFOpen biology · 2018Article
- A facilitated diffusion model constrained by the probability isotherm: a pedagogical exercise in intuitive non-equilibrium thermodynamics.Royal Society open science · 2017Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The H(+)/ATP ratio is an important parameter for the energy balance of all cells and for the coupling mechanism between proton transport and ATP synthesis. A straightforward interpretation of rotational catalysis predicts that the H(+)/ATP coincides with the ratio of the c-subunits to beta-subunits, implying that, for the chloroplast and Escherichia coli ATPsynthases, numbers of 4.7 and 3.3 are expected. Here, the energetics described by the chemiosmotic theory was used to determine the H(+)/ATP ratio for the two enzymes. The isolated complexes were reconstituted into liposomes, and parallel measurements were performed under identical conditions. The internal phase of the liposomes was equilibrated with the acidic medium during reconstitution, allowing to measure the internal pH with a glass electrode. An acid-base transition was carried out and the initial rates of ATP synthesis or ATP hydrolysis were measured with luciferin/luciferase as a function of DeltapH at constant Q = [ATP]/([ADP][P(i)]). From the shift of the equilibrium DeltapH as a function of Q the standard Gibbs free energy for phosphorylation, DeltaG(p)(0)'; and the H(+)/ATP ratio were determined. It resulted DeltaG(p)(0)' = 38 +/- 3 kJ.mol(-1) and H(+)/ATP = 4.0 +/- 0.2 for the chloroplast and H(+)/ATP = 4.0 +/- 0.3 for the E. coli enzyme, indicating that the thermodynamic H(+)/ATP ratio is the same for both enzymes and that it is different from the subunit stoichiometric ratio.
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