Evidence map›Paper›PMID 20193659›Full record

ReviewBiochimica et biophysica acta2010

F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.

David B Hicks, Jun Liu, Makoto Fujisawa, Terry A Krulwich

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. ATP synthase activity boosts membrane proton acceptance and lateral diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Indian journal of microbiology · 2025
    Article
  4. HFrontiers in microbiology · 2025
    Review
  5. Saline-Alkali Soil Property Improved by the Synergistic Effects ofInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Why Nature Chose Potassium.Journal of molecular evolution · 2019
    Review
  16. Recent advances of pH homeostasis mechanisms in Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2019
    Review
  17. Draft Genome Sequence of Alkalicoccus saliphilus DSM 15402Microbiology resource announcements · 2019
    Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

David B HicksDepartment of Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine, New York, NY 10029, USA. david.hicks@mssm.edu
Jun Liu
Makoto Fujisawa
Terry A Krulwich
Icahn School of Medicine at Mount Sinai · USToyo University · JP

Funding

PROTON COUPLING STRATEGIES IN ALKALIPHILIC BACILLUSR01GM028454 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KRULWICH, TERRY ANN · 1985 to 2017
$6.2M
NIGMS NIH HHS GM28454NIGMS NIH HHS R01 GM028454
6 · The paper itself

Abstract

This review focuses on the ATP synthases of alkaliphilic bacteria and, in particular, those that successfully overcome the bioenergetic challenges of achieving robust H+-coupled ATP synthesis at external pH values>10. At such pH values the protonmotive force, which is posited to provide the energetic driving force for ATP synthesis, is too low to account for the ATP synthesis observed. The protonmotive force is lowered at a very high pH by the need to maintain a cytoplasmic pH well below the pH outside, which results in an energetically adverse pH gradient. Several anticipated solutions to this bioenergetic conundrum have been ruled out. Although the transmembrane sodium motive force is high under alkaline conditions, respiratory alkaliphilic bacteria do not use Na+- instead of H+-coupled ATP synthases. Nor do they offset the adverse pH gradient with a compensatory increase in the transmembrane electrical potential component of the protonmotive force. Moreover, studies of ATP synthase rotors indicate that alkaliphiles cannot fully resolve the energetic problem by using an ATP synthase with a large number of c-subunits in the synthase rotor ring. Increased attention now focuses on delocalized gradients near the membrane surface and H+ transfers to ATP synthases via membrane-associated microcircuits between the H+ pumping complexes and synthases. Microcircuits likely depend upon proximity of pumps and synthases, specific membrane properties and specific adaptations of the participating enzyme complexes. ATP synthesis in alkaliphiles depends upon alkaliphile-specific adaptations of the ATP synthase and there is also evidence for alkaliphile-specific adaptations of respiratory chain components.

Indexed as

Adaptation, PhysiologicalAdenosine TriphosphateAmino Acid SequenceBacillusBacteriaEnergy MetabolismHydrogen-Ion ConcentrationMolecular Sequence DataPhosphorylationProton-Translocating ATPasesAdenosine TriphosphateProton-Translocating ATPases

Identifiers

PMID20193659
PMCPMC2890045
OpenAlexW2002695373

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.