According to the Williams model, the work of mitochondrial respiratory H+ pumps gives rise to a fraction of membrane-bound protons (R-protons) that have excess free energy, which is used in the reaction of ATP synthesis. We have earlier managed to detect such a fraction in mitochondria and mitoplasts and to rigorously show (for mitoplasts) that the non-equilibrium R-proton fraction is localized on the surface of the inner membrane. Here we show that a surface-active compound 2,4,6-trichloro-3-pentadecylphenol anion (TCP-C15) selectively interacts with the R-proton fraction, and describe in detail its influence on mitochondrial respiration under conditions of R-proton generation. We also report endogenous regulation of the R-proton fraction volume, which is performed by the phosphate transport system. The results are discussed in terms of the local coupling model.
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Original Russian Text © L.S. Yaguzhinsky, K.A. Motovilov, E.M. Volkov, S.A. Eremeev, 2013, published in Biofizika, 2013, Vol. 58, No. 1, pp. 117–125.
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Yaguzhinsky, L.S., Motovilov, K.A., Volkov, E.M. et al. Interaction of a surface-active base with the fraction of membrane-bound Williams’ protons. BIOPHYSICS 58, 95–102 (2013). https://doi.org/10.1134/S0006350913010181
- surface-active phenols
- local coupling
- adenine nucleotide translocator
- phosphate transport