Evidence map›Paper›PMID 26483483›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.

Sándor Volkán-Kacsó, Rudolph A Marcus

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023
    Review
  4. Article
  5. FFrontiers in microbiology · 2022
    Review
  6. Rotary catalysis of bovine mitochondrial FProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Method to extract multiple states in FProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Insights into the origin of the high energy-conversion efficiency of FProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Theory of long binding events in single-molecule-controlled rotation experiments on FProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Inseparable tandem: evolution chooses ATP and Ca2+ to control life, death and cellular signalling.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  14. F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. Brønsted slopes based on single-molecule imaging data help to unveil the chemically coupled rotation in F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Sándor Volkán-KacsóNoyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125.
Rudolph A MarcusNoyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125 ram@caltech.edu.
California Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A theoretical model of elastically coupled reactions is proposed for single molecule imaging and rotor manipulation experiments on F1-ATPase. Stalling experiments are considered in which rates of individual ligand binding, ligand release, and chemical reaction steps have an exponential dependence on rotor angle. These data are treated in terms of the effect of thermodynamic driving forces on reaction rates, and lead to equations relating rate constants and free energies to the stalling angle. These relations, in turn, are modeled using a formalism originally developed to treat electron and other transfer reactions. During stalling the free energy profile of the enzymatic steps is altered by a work term due to elastic structural twisting. Using biochemical and single molecule data, the dependence of the rate constant and equilibrium constant on the stall angle, as well as the Børnsted slope are predicted and compared with experiment. Reasonable agreement is found with stalling experiments for ATP and GTP binding. The model can be applied to other torque-generating steps of reversible ligand binding, such as ADP and Pi release, when sufficient data become available.

Indexed as

Models, ChemicalMolecular Dynamics SimulationAdenosine DiphosphateAdenosine TriphosphateGuanosine TriphosphateProtein BindingProton-Translocating ATPasesThermodynamicsAdenosine DiphosphateAdenosine TriphosphateGuanosine TriphosphateProton-Translocating ATPasesATPasebiomolecular motorsBrønsted slopefree energy relationssingle molecule imaging

Identifiers

PMID26483483
PMCPMC4655567
OpenAlexW2120624013

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.