FOF1-ATPase mediates regulation of fermentation and energy metabolism at pH 5.5.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: FOF1-ATPase mediates regulation of fermentation and energy metabolism at pH 5.5.
Συγγραφείς: Gevorgyan H; Department of Biochemistry, Microbiology and Biotechnology, Faculty of Biology, Yerevan State University, 0025, Yerevan, Armenia.; Scientific-Research Institute of Biology, Faculty of Biology, Yerevan State University, 1 A. Manoogian Str., 0025, Yerevan, Armenia.; Microbial Biotechnologies and Biofuel Innovation Center, Yerevan State University, 0025, Yerevan, Armenia., Trchounian K; Department of Biochemistry, Microbiology and Biotechnology, Faculty of Biology, Yerevan State University, 0025, Yerevan, Armenia. k.trchounian@ysu.am.; Scientific-Research Institute of Biology, Faculty of Biology, Yerevan State University, 1 A. Manoogian Str., 0025, Yerevan, Armenia. k.trchounian@ysu.am.; Microbial Biotechnologies and Biofuel Innovation Center, Yerevan State University, 0025, Yerevan, Armenia. k.trchounian@ysu.am.
Πηγή: Scientific reports [Sci Rep] 2025 Oct 14; Vol. 15 (1), pp. 35873. Date of Electronic Publication: 2025 Oct 14.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE
Imprint Name(s): Original Publication: London : Nature Publishing Group, copyright 2011-
Ιατρικοί όροι (MeSH): Escherichia coli*/metabolism , Escherichia coli*/enzymology , Escherichia coli*/genetics , Proton-Translocating ATPases*/metabolism , Proton-Translocating ATPases*/genetics , Escherichia coli Proteins*/metabolism , Escherichia coli Proteins*/genetics , Fermentation* , Energy Metabolism*, Glucose/metabolism ; Formates/metabolism ; Glycerol/metabolism ; Hydrogen/metabolism ; Hydrogen-Ion Concentration ; Proton-Motive Force
Περίληψη: The activity of FOF1-ATP synthase (FOF1) is vital for the survival and anaerobic growth under acidic conditions providing efficient metabolism and energy for cellular function. This study demonstrated the role of FOF1-ATPase in the metabolic pathways and regulation of proton motive force in Escherichia coli at pH 5.5 during the fermentation of glucose, glycerol and formate. Alteration of the ratio of fermentation end-products was shown. The possible mechanisms for efficient energy utilization in cells lacking FOF1 were shown. It is suggested that Fdh-H transfers H+ from formate to Hyd, which serves not only for H₂ generation but also for H+ cycling to FOF1 or directly to FOF1 in cells grown for 20 h. The interaction between H2 and H+ cycling was proposed as an essential mechanism for balancing ΔpH at acidic conditions. FOF1-ATPase was identified to play a pivotal role in forming both components of Δp at 20 h and 72 h.
(© 2025. The Author(s).)
Competing Interests: Declarations. Competing interests: The authors declare no competing interests.
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Grant Information: 23LCG-1F003 State Committee of Science
Contributed Indexing: Keywords: Acidic pH; FOF1-ATPase; Proton and hydrogen cycling; Proton conductance; Proton motive force; Proton permeability
Substance Nomenclature: EC 3.6.3.14 (Proton-Translocating ATPases)
IY9XDZ35W2 (Glucose)
0 (Formates)
PDC6A3C0OX (Glycerol)
0YIW783RG1 (formic acid)
7YNJ3PO35Z (Hydrogen)
0 (Escherichia coli Proteins)
Entry Date(s): Date Created: 20251014 Date Completed: 20251014 Latest Revision: 20251017
Update Code: 20260130
PubMed Central ID: PMC12521522
DOI: 10.1038/s41598-025-21047-w
PMID: 41087635
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:2045-2322
DOI:10.1038/s41598-025-21047-w