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Theorem of inevitable death: calibration of the universal dissipative metabolism model on human ATP synthase
2026-03-13
This work presents an experimental calibration of a universal dissipative metabolism model describing the dynamics of three fundamental state parameters — resource m, variability g, and consolidation k. The model is based on the concept of a metabolic power quantum P as an atomic portion of negentropy flow and includes theorems on inevitable death, survival criterion, and fluctuation spectral density isomorphic to Planck's formula. Based on structural data of human ATP synthase (EMDB ID EMD-34572, PDB ID 8H9L) and modern biophysical studies, empirical calibration of key parameters was performed: reinvestment efficiency, variability constant, quantum energy. The characteristic frequency of the fluctuation spectrum was obtained, corresponding to the mid-IR range. E. Schrodinger's principle (1944) on the suppression of quantum fluctuations in large molecular aggregates is quantitatively confirmed: it is shown that the isolated c-ring reaches the theoretical quantum rotation limit, but within the whole enzyme, rotation slows down by 1–3 orders of magnitude due to collective effects. The obtained values can be directly substituted into the model's dynamic equations for quantitative modeling of evolutionary, biological, and social processes.
Ссылка для цитирования:
Polyukov P. 2026. Theorem of inevitable death: calibration of the universal dissipative metabolism model on human ATP synthase. PREPRINTS.RU. https://doi.org/10.24108/preprints-3114689
Список литературы
1. Polyukov P. A. 2026. Theorem of inevitable death: dissipative cycle, reinvestment and survival criterion for complex systems. PREPRINTS.RU.\\ https://doi.org/10.24108/preprints-3114519
2. Lai Y., Zhang Y., Zhou S., Xu J., Du Z., Feng Z., Yu L., Zhao Z., Wang W., Tang Y., Yang X., Guddat L.W., Liu F., Gao Y., Rao Z., Gong H. Structure of the human ATP synthase // Molecular Cell. 2023. Vol. 83, No. 12. P. 2137-2147. DOI: 10.1016/j.molcel.2023.04.029. (EMDB ID EMD-34572, PDB ID 8H9L)
3. Dimroth P., von Ballmoos C., Meier T. Catalytic and mechanical cycles in F-ATP synthases // EMBO Reports. 2006. Vol. 7, No. 3. P. 276-282. DOI: 10.1038/sj.embor.7400646
4. Matar I.K., Fahimi P., Matta C.F. Rotational Dynamics of ATP Synthase: Mechanical Constraints and Energy Dissipative Channels // Pure and Applied Chemistry. 2025. Vol. 97, No. 10. P. 1-14. DOI: 10.1515/pac-2025-0477
5. Nath S. Novel molecular insights into ATP synthesis in oxidative phosphorylation based on the principle of least action // Chemical Physics Letters. 2022. Vol. 796. Article 139561. DOI: 10.1016/j.cplett.2022.139561
6. Stoichiometry of the respiratory chain // WikiLectures. 2022.\\ https://www.wikilectures.eu/w/Stoichiometry_of_the_respiratory_chain
7. Schrodinger E. What Is Life? The Physical Aspect of the Living Cell. Cambridge: Cambridge University Press, 1944.
8. Matar I.K., Fahimi P., Matta C.F. Rotational Dynamics of ATP Synthase: Mechanical Constraints and Energy Dissipative Channels // arXiv. 2025. arXiv:2506.23439v1.
9. Biology Stack Exchange. Where does the additional 1 proton cost of oxidative phosphorylation come from? 2019. https://biology.stackexchange.com/questions/80465/where-does-the-additional-1-proton-cost-of-oxidative-phosphorylation-come-from
10. RCSB PDB - 8H9L: Human ATP synthase F1 domain, state 3a.\\ https://www.rcsb.org/structure/8H9L (accessed 2026)
