Finding. Protons that feed ATP synthase are not supposed to vanish into the intermembrane-space water. Adeniran and Degens build a two-dimensional continuum model tight enough to stop the usual parameter shrug. They lock buffer consumption to experimental rates, fit time-resolved DOPG fluorescence, and split the trap: 5.7 kT from interfacial water, 4.3 kT from a monovalent lipid’s −1e charge. Cardiolipin carries −2e. The model then digs a 14.3 kT well, holds protons 1 to 2 nanometres from the membrane, kills vertical leak, and, by squeezing the dimension, speeds the lateral wave toward ATP synthase. They call the lipid a nanoscale antenna.
Why this paper matters
Localized versus delocalized chemiosmosis is an old fight. This is a number, not a slogan. If cardiolipin’s extra charge is worth ~14 kT, Barth syndrome and other cardiolipin defects are proton-antenna diseases as well as cristae-shape diseases. Respiratory-chain kinetics that assume bulk pH in the IMS will be too slow.
How to read the score
High eighties. Core bioenergetics, a clean decomposition, a cardiolipin prediction. Confidence is medium: extrapolation from DOPG, planar geometry, no protein.
Caveats
A well-posed model can still be wrong in a crista. Do not quote 14.3 kT as a measured mitochondrial number.
What to do with it
If you simulate proton circuits, put a 1–2 nm cardiolipin slab in. If you work on cardiolipin disease, add antenna failure to the phenotype list. Read the DOPG calibration before you reuse the kT split.