Mitochondrial energetics has now been much better elucidated, for the first time, using a newly formulated equation for protonic motive force (pmf) across a biological membrane that takes electrostatically localized protons into account using experimental data for animal mitochondria. The elucidation showed that the localized protons dominate the total pmf. It is also surprisingly discovered that the local pmf from the isothermal utilization of latent heat enthalpy through the localized protons is not constrained by the overall energetics of the redox-driven proton pump system because (i) the localized protons are not free to move away from the membrane surface, (ii) the redox-driven proton pumps embedded in the mitochondrial membrane extend beyond the localized proton layer, and (iii) the protonic inlet mouth of the ATP synthase that accepts protons is located within this layer. Remarkably, this explanation agrees well with the true protein complex structures of mitochondrial respiratory-coupling sites. Therefore, it is now quite clear that mitochondria are able to isothermally utilize the latent heat effectively through electrostatically localized protons to synthesize ATP. Mitochondria-powered organisms are not only chemotrophs but also thermotrophs that can create significant amounts of Gibbs free energy through isothermal utilization of latent heat energy to do work such as driving ATP synthesis.

Mitochondrial energetics with electrostatically localized protons: Do we have a thermotrophic feature?

2019 Spring National Meeting

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