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Cited by 54ATP Synthase and ATPases ResearchMitochondrial Function and PathologyPhotosynthetic Processes and Mechanisms

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An exploration of how the thermodynamic efficiency of bioenergetic membrane systems varies with c-subunit stoichiometry of F1F0 ATP synthases

Silverstein, Todd P.·2014·Journal of Bioenergetics and Biomembranes
DOI 10.1007/s10863-014-9547-y
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Abstract

Recently the F0 portion of the bovine mitochondrial F1F0-ATP synthase was shown to contain eight 'c' subunits (n = 8). This surprised many in the field, as previously, the only other mitochondrial F0 (for yeast) was shown to have ten 'c' subunits. The metabolic implications of 'c' subunit copy number explored in this paper lead to several surprising conclusions: (1) Aerobically respiring E. coli (n = 10) and animal mitochondria (n = 8) both have very high F1F0 thermodynamic efficiencies of ≈90% under typical conditions, whereas efficiency is only ≈65% for chloroplasts (n = 14). Reasons for this difference, including the importance of transmembrane potential (∆Ψ) as a rotational catalyst, as opposed to an energy source, are discussed. (2) Maximum theoretical P/O ratios in animal mitochondria (n = 8) are calculated to be 2.73 ATP/NADH and 1.64 ATP/FADH2, yielding 34.5 ATP/glucose (assuming NADH import via the malate/aspartate shuttle). The experimentally measured values of 2.44 (±0.15), 1.47 (±0.13), and 31.3 (±1.5), respectively, are only about 10% lower, suggesting very little energy depletion via transmembrane proton leakage. (3) Finally, the thermodynamic efficiency of oxidative phosphorylation is not lower than that of substrate level phosphorylation, as previously believed. The overall thermodynamic efficiencies of oxidative phosphorylation, glycolysis, and the citric acid cycle are ≈80% in all three processes.

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Metadata

Authors
Silverstein, T. P.
Affiliations
Willamette University (US)
Corresponding author
Silverstein, Todd P.
ORCID
Silverstein, Todd P.
Venue
Journal of Bioenergetics and Biomembranes
Publisher
Springer Science and Business Media LLC
Published
2014-04-06
Volume
46
Issue
3
Pages
229-241
ISSN
  • 0145-479X (ISSN-L)
  • 1573-6881
DOI
10.1007/s10863-014-9547-y
OpenAlex
W2064715954
Cited by
54
References
1
Citations by year
2025: 8 · 2024: 4 · 2023: 7 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 1 · 2016: 6 · 2015: 5 · 2014: 1
FWCI
1.78
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Journal of Bioenergetics and Biomembranes (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Keywords
F0F1-ATP synthase, thermodynamic efficiency, proton leak, membrane potential, P/O ratio, oxidative phosphorylation, substrate-level phosphorylation, chloroplast ATP synthase, malate-aspartate shuttle, glycolysis, TCA cycle
MeSH terms
Animals, Computer Simulation, Energy Transfer, Humans, Models, Biological, Oxygen, Structure-Activity Relationship, Thermodynamics, Protein Subunits, Mitochondrial Proton-Translocating ATPases, Mitochondrial Membranes

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Silverstein, T. P. (2014). An exploration of how the thermodynamic efficiency of bioenergetic membrane systems varies with c-subunit stoichiometry of F1F0 ATP synthases. Journal of Bioenergetics and Biomembranes. https://doi.org/10.1007/s10863-014-9547-y

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