Isothermal Environmental Heat Energy Utilization by Transmembrane Electrostatically Localized Protons at the Liquid–Membrane Interface

This
study employing the latest theory on transmembrane electrostatic
proton localization has now, for the first time, consistently elucidated
a decades-longstanding bioenergetic conundrum in alkalophilic bacteria
and more importantly discovered an entirely new feature: isothermal
environmental heat utilization by electrostatically localized protons
at the liquid–membrane interface. It was surprisingly revealed
that the protonic motive force (equivalent to Gibbs free energy) from
the isothermal environmental heat energy utilization through the electrostatically
localized protons is not constrained by the overall energetics of
the redox-driven proton pump system because of the following: (a)
the transmembrane electrostatically localized protons are not free
to move away from the membrane surface as a protonic capacitor feature;
(b) the proton pumps embedded in the cell membrane extend beyond the
localized proton layer apparently as an asymmetric property of the
biological membrane; and (c) the protonic inlet mouth of the ATP synthase
that accepts protons is located within this layer as another natural
property of the asymmetric biological membrane. This work has now,
for the first time, shown a novel thermotrophic feature where biological
systems can isothermally utilize environmental heat energy through
transmembrane electrostatically localized protons to help drive ATP
synthesis.