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In FOF1 ATP synthase, driven by the proton motive force across the membrane, the FO motor rotates the central rotor and induces conformational changes in the F1 motor, resulting in ATP synthesis. Recently, many near-atomic resolution structural models have been obtained using cryo-electron microscopy. Despite high …

… How could the primordial “pre-life” entity have the ability to control its inside as well as outside for maintaining trans-membrane potential (TMP; including proton-motive force or pmf) before such a complex membrane could have ever developed? How can contemporary cells continue to do so, even …

… Because ATP synthase requires Pi as substrate, Pi availability—and thus TPT-mediated return—feeds back onto ATP production from pmf, providing another route by which carbon-export status influences how proton-motive energy is cashed out (Cruz et al., 2001; Golding and Johnson, 2003).

This review describes a proton-centric view of leaf photosynthesis in which the partitioning of the thylakoid proton motive force (pmf)—the balance between ΔpH and Δψ—links light harvesting, ATP synthesis, photoprotection, and downstream carbon metabolism. Proton pumps in LEF and CEF build pmf; ATP synthase and …

This gradient produces the proton motive force (PMF or ∆p), which can be described as a measure of the potential energy stored across the IMM. Since protons are electrically charged particles, the PMF has both chemical and electric components. The electric component corresponds to the voltage difference across …

ATP synthesis by the action of FOF1 ATP synthase is driven by the proton motive force, which is the sum of contributions from the proton concentration gradient and membrane electrical potential as pointed out by Mitchell (1961). For the former, the pH values on the IMS and matrix …

… This generates the proton-motive force, which is composed of both a pH gradient and the mitochondrial membrane potential (ΔΨm) [4] allowing ATP synthase (complex V) to harnesses this electrochemical gradient to produce ATP.

In durum wheat mitochondria (DWM) the ATP-inhibited plant mitochondrial potassium channel (PmitoKATP) and the plant uncoupling protein (PUCP) are able to strongly reduce the proton motive force (pmf) to control mitochondrial production of reactive oxygen species; under these conditions, mitochondrial carriers lack the driving force for transport …

… In leaves, the immediate energetic intermediate that links light-driven electron transfer to ATP synthesis is the proton motive force (pmf, ΔμH+) across the thylakoid membrane. Water oxidation at photosystem II (PSII) and proton-coupled plastoquinol oxidation at the cytochrome b6f complex deposit protons into the thylakoid lumen …

… The fact that the proton-motive force is more universal today than the sodium-motive force probably derives from evolutionary interpolation of quinones—which are always coupled to proton-dependent redox reactions—on these earlier, necessarily promiscuous origins [205].

… The reversed gradient reduces the trans-membrane proton-motive force available to energize ATP synthesis.

… In chloroplasts, this balance is strongly governed by the thylakoid proton motive force (pmf, ΔμH+) and by its partitioning between a pH gradient (ΔpH) and an electric field (Δψ). A proton-circuit framework in which proton deposition by linear and cyclic electron flow builds pmf, chloroplast ATP synthase …

… The resulting loss in proton motive force prevents ADP phosphorylation to ATP at the level of ATP synthase, which rather works in “reverse mode” coupling ATP hydrolysis to proton pumping. The net result is that mitochondria no longer produce ATP and become very powerful in hydrolyzing glycolytic ATP …

… c in a reaction sequence that is referred to as the proton-motive Q-cycle, which contributes to maintaining the proton electrochemical potential across the inner mitochondrial membrane.86 The QH2 electron donor binds in a Q-binding site referred to as QP, which is located near the …

The thylakoid proton motive force (pmf, ΔμH+) is the electrochemical driving force for proton movement across the thylakoid membrane. It can be decomposed into two thermodynamic components: a transmembrane electric potential (Δψ) and a pH gradient (ΔpH). Although Δψ and ΔpH are thermodynamically interchangeable contributors to ΔμH+, they …

… The resulting proton motive force drives the rotation of the FO sector of ATP synthase leading to the synthesis of ATP in the F1 sector, but the electron flow through the respiratory chain also generates ROS/RNS. In addition, the mitochondrial permeability transition pore (PTP), a large-conductance …

… Complex V (adenosine-5′-triphosphate synthase) utilizes the transmembrane proton-motive force ΔμH+, generated by respiration, to drive the synthesis of ATP from ADP and inorganic phosphate. The monomeric complex V is made up of two domains, a membrane embedded portion (so-called Fo), through which transmembrane proton …

… This gives rise to a latent Δp (proton motive force) and a reserve adenine pool, two key components required for ATP synthesis by F0F1-ATP synthase. As the concentration of inorganic phosphate (Pi) within IMS increases beyond a threshold level (Figure 2A), the synthetic activity of PNPase ceases …

… The negatively charged surface operates as a transient proton sink amplifying the proton motive force and increasing ATP level two to five times compared to ATP levels in corresponding planktonic cells [12]. Underlying this phenomenon of enhanced ATP production is enrichment of H+ in the vicinity of a …

… The finding that such alkaliphilic aerobes use proton-coupled ATP synthases was a surprising finding, since the apparently low bulk proton-motive force (PMF) had led to the expectation that synthesis would be coupled to larger bulk sodium-ion gradients (Hicks and Krulwich, 1990; Krulwich, 1995). The use …