TELP theory: Elucidating the major observations of Rieger et al. 2021 in mitochondria

Abstract

The transmembrane-electrostatically localized protons (TELP) theory may represent a complementary development to Mitchell's chemiosmotic theory. The combination of the two together can now excellently explain the energetics in mitochondria. My calculated transmembrane-attractive force between an excess proton and an excess hydroxide explains how TELP may stay within a 1-nm thin layer at the liquid-membrane interface. Consequently, any pH sensor (sEcGFP) located at least 2–3 nm away from the membrane surface will not be able to see TELP. This feature as predicted from the TELP model was observed exactly in the experiment of Rieger et al., 2021. In contrast to their belief “the Δp at ATP synthase is almost negligible under OXPHOS conditions”, I find, when TELP activity is included in the energy calculations, there is plenty of total protonic Gibbs free energy ($\Delta G_T$) well above the physiologically required value of −24.5 kJ mol⁻¹ to drive ATP synthesis through F_oF₁-ATP synthase.