Proton Motive Force Regulation in Bacterial Membranes
Summary
Bacteria exploit the proton motive force (PMF) as a central energy currency, harnessing the electrochemical gradient of protons across the cytoplasmic membrane to drive ATP synthesis, nutrient uptake and ion homeostasis. PMF arises from two interdependent components: a transmembrane pH difference (ΔpH) and an electrical potential (Δψ). Cells regulate PMF dynamically by modulating respiratory chain activity, proton‐translocating ATPases and secondary transporters. Under conditions of nutrient limitation or environmental stress, bacteria adjust expression and assembly of F₁F₀‐ATP synthases, proton‐antiporters and symporters to maintain cytoplasmic pH and membrane potential. Fine‐tuning of proton leak pathways, lipid composition and ion channels further stabilises PMF, linking metabolic state to motility, biofilm formation and virulence.
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Proton Motive Force Regulation in Bacterial Membranes publication trend
The graph below shows the total number of articles in proton motive force regulation in bacterial membranes across all publications each year (not limited to Nature Index journals).
Technical terms
Proton motive force (PMF): The combined electrochemical gradient of protons (ΔpH and Δψ) across a membrane that stores energy for cellular processes.
Δψ (membrane potential): The electrical potential difference between the cytoplasm and the exterior, arising from asymmetric ion distribution.
F₁F₀‐ATPase: A multi‐subunit rotary enzyme complex that synthesises or hydrolyses ATP by translocating protons across the membrane.
Symport: Co‐transport mechanism in which a substrate is carried across the membrane together with one or more protons down the PMF.
Chemiosmotic hypothesis: Theory that biological energy conversion relies on coupling of electron transport to proton translocation, generating PMF to drive ATP synthesis and transport.
References
- Accumulation of Neutral Amino Acids by Streptococcus faecalis ENERGY COUPLING BY A PROTON-MOTIVE FORCE. Journal of Biological Chemistry (1973).
- Mechanism of proline transport in Escherichia coli K12. I. Effect of a membrane potential on the kinetics of 2H+/proline symport in cytoplasmic membrane vesicles.. Journal of Biological Chemistry (1984).
- Energy Coupling in Membrane Vesicles of Escherichia coli I. ACCUMULATION OF METABOLITES IN RESPONSE TO AN ELECTRICAL POTENTIAL. Journal of Biological Chemistry (1974).
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