ArticleProceedings of the National Academy of Sciences of the United States of America2022
ATP synthesis in an ancient ATP synthase at low driving forces.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Formate- and Sodium Ion-Dependent Wood-Ljungdahl Pathway Involved in Organo-, Litho-, and Methylotrophic Growth of Tepidanaerobacter acetatoxydans.Environmental science & technology · 2026Article
- Methanol Metabolism in the Cytochrome and Menaquinone-Containing Acetogen Moorella thermoacetica.Environmental microbiology · 2026Article
- Chaperone-mediated thermotolerance in hyperthermophilic composting: Molecular-Level protein remodeling of microbial communities.Environmental science and ecotechnology · 2025Article
- ATP synthesis of Enterococcus hirae V-ATPase driven by sodium motive force.The Journal of biological chemistry · 2025Article
- Unexpected metabolic rewiring of COProceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hyperthermophilic archaea are close to the origin of life. Some hyperthermophilic anaerobic archaea live under strong energy limitation and have to make a living near thermodynamic equilibrium. Obviously, this requires adaptations of the energy-conserving machinery to harness small energy increments. Their ATP synthases often have an unusual motor subunit c that is predicted to prevent ATP synthesis. We have purified and reconstituted into liposomes such an archaeal ATP synthase found in a mesophilic bacterium. The enzyme indeed synthesized ATP at physiological membrane potentials, despite its unusual c subunit, but the minimal driving force for ATP synthesis was found to be even lower than in ATP synthases with usual c subunits. These data not only reveal an intermediate in the transition from ATP hydrolases to ATP synthases but also give a rationale for a bioenergetic adaptation of microbial growth near the thermodynamic equilibrium.
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Registered trials
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