Abstract

Through the application of a new transmembrane electrostatic proton localization theory in mitochondria, it was surprisingly discovered with well-corroborated evidences that the local protonic motive force represents a novel bioenergetic phenomenon: isothermal utilization of environmental heat energy through the electrostatically localized protons at the mitochondrial cristae liquid-membrane interface. This energy transduction phenomenon is not constrained by the overall energetics of the redox-driven proton pump system in mitochondria through at least one of following mechanisms: (1) the geometric effect of mitochondrial cristae in enhancing the density of localized protons at the cristae tips where the ATP synthase enzymes are located; (2) the transmembrane electrostatically localized protons not free to move away from the liquid-membrane interface; (3) the redox-driven proton pumps embedded in the mitochondrial membrane protruded beyond localized proton layer; and (4) the ATP synthase protonic inlet mouth located within this localized proton layer.

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