Academic Journal

ATP synthase activity boosts membrane proton acceptance and lateral diffusion.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: ATP synthase activity boosts membrane proton acceptance and lateral diffusion.
Συγγραφείς: Flegel H; Faculty of Chemistry, Institute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen 37077, Germany., Variyam AR; Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 3200003, Israel., Amdursky N; Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 3200003, Israel.; Chemistry, School of Mathematical and Physical Sciences, University of Sheffield, Sheffield S3 7HF, United Kingdom., Steinem C; Faculty of Chemistry, Institute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen 37077, Germany.
Πηγή: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2026 Mar 10; Vol. 123 (10), pp. e2510444123. Date of Electronic Publication: 2026 Mar 03.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
Imprint Name(s): Original Publication: Washington, DC : National Academy of Sciences
Ιατρικοί όροι (MeSH): Proton-Translocating ATPases*/metabolism , Cell Membrane*/metabolism , Protons*, Adenosine Triphosphate/metabolism ; Bacillus/enzymology ; Lipid Bilayers/metabolism ; Lipid Bilayers/chemistry ; Unilamellar Liposomes/metabolism ; Diffusion ; Proton-Motive Force ; Spectrometry, Fluorescence
Περίληψη: In most organisms, ATP synthesis is powered by the proton motive force (pmf) and catalyzed by ATP synthase. While the chemiosmotic theory originally proposed a "delocalized coupling" between proton pumps and consumers, growing evidence implicates the membrane in mediating localized proton transfer (PT). To directly track ultrafast PT at the membrane surface as a function of ATP synthase activity, we developed an in vitro system. We tethered a light-activated excited-state photoacid to the bilayer of unilamellar vesicles to confine PT to the membrane interface and co-reconstituted a thermophilic Bacillus TFOF1 ATP synthase. Using steady-state and time-resolved fluorescence spectroscopy, we quantified PT and lateral proton diffusion from the anchored photoacid under conditions with non-ATP- and ATP-producing enzymes. Our results show that the membrane accepts protons at its interface and that PT is enhanced only when ATP synthase is active. A comparison with soluble photoacid positioned near the membrane shows that protons consumed by ATP synthase do not equilibrate with the bulk aqueous phase. Instead, they are transferred directly along the two-dimensional membrane interface to the enzyme. This localized coupling can explain how ATP synthesis can proceed even when the apparent bulk pmf seems insufficient. Our results refine the proton translocation during ATP synthesis by revealing that the membrane itself is an active participant in PT, thereby strengthening the case for localized proton coupling in bioenergetics.
Competing Interests: Competing interests statement:The authors declare no competing interest.
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Grant Information: grant no. 76251-10-4/20 (ZN 3625) Volkswagen Foundation (VolkswagenStiftung)
Contributed Indexing: Keywords: HPTS; energy conversion; proton transfer; time-correlated single photon counting; unilamellar vesicles
Substance Nomenclature: 0 (Protons)
8L70Q75FXE (Adenosine Triphosphate)
EC 3.6.3.14 (Proton-Translocating ATPases)
0 (Lipid Bilayers)
0 (Unilamellar Liposomes)
Entry Date(s): Date Created: 20260303 Date Completed: 20260710 Latest Revision: 20260813
Update Code: 20260813
PubMed Central ID: PMC12974407
DOI: 10.1073/pnas.2510444123
PMID: 41774794
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:1091-6490
DOI:10.1073/pnas.2510444123