Academic Journal
ATP synthase activity boosts membrane proton acceptance and lateral diffusion.
| 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 TF |
| 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 |
| ISSN: | 1091-6490 |
|---|---|
| DOI: | 10.1073/pnas.2510444123 |