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… Changes in environmental pH can significantly modulate the proton motive force (PMF), depends on the membrane potential (ΔΨ) and the transmembrane proton gradient (ΔpH), both of which drive the catalytic cycle of proton-dependent efflux pumps such as AcrAB–TolC. Changes in extracellular or cytoplasmic pH may therefore …

… 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 …

… Nodulation–Division (RND) family efflux pumps, such as AcrAB–TolC in Escherichia coli and Salmonella spp., which are powered by the proton motive force (PMF) across the inner membrane, are tripartite complexes that span the Gram-negative cell envelope to actively expel toxic compounds including antibiotics (Gaurav et …

… 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 RND family, primarily found in Gram-negative bacteria, includes tripartite assemblies such as AcrAB-TolC, which expel a wide range of antibiotics and toxic compounds using the proton motive force for energy (Chetri, 2023; Duffey et al., 2024). The MFS pumps are ubiquitous across bacterial species, functioning …

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

The catalytic cycles of multidrug efflux pumps, especially those in the RND and MFS families, are tightly coupled to the proton motive force (PMF) across the bacterial cytoplasmic membrane (Chetri, 2023; Li et al., 2024). This energy is transduced by dedicated proton relay networks within the inner membrane …

… 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 …

… Each AcrB protomer consists of three domains—the transmembrane domain (TMD), which harnesses the proton motive force to energize transport, the porter domain (PD) responsible for substrate recognition and binding, and the funnel domain (FD) that interfaces with AcrA (Vargiu et al., 2022). The pump operates through a …

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 …