Evidence map›Paper›PMID 26537397›Full record

ReviewQuarterly reviews of biophysics2015

Torque, chemistry and efficiency in molecular motors: a study of the rotary-chemical coupling in F1-ATPase.

Shayantani Mukherjee, Ram Prasad Bora, Arieh Warshel

Open access · hybridAbstract readReview
In one paragraph

Review in Quarterly reviews of biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024
    Article
  3. Article
  4. Mechanochemical active ratchet.Scientific reports · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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
  10. Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. The FPhotosynthesis research · 2017
    Review
  12. Article
  13. Simulating the dynamics of the mechanochemical cycle of myosin-V.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. The Physics and Physical Chemistry of Molecular Machines.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016
    Review
  15. Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. 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

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

3 authors at 1 institution in 1 country.

Shayantani MukherjeeDepartment of Chemistry,University of Southern California,418 SGM Building,3620 McClintock Avenue,Los Angeles,CA 90089-1062,USA.
Ram Prasad BoraDepartment of Chemistry,University of Southern California,418 SGM Building,3620 McClintock Avenue,Los Angeles,CA 90089-1062,USA.
Arieh WarshelDepartment of Chemistry,University of Southern California,418 SGM Building,3620 McClintock Avenue,Los Angeles,CA 90089-1062,USA.
University of Southern California · US

Funding

Mechanistic Analysis of Pol Beta and Cancer-Associated MutantsU19CA105010 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2004 to 2012
$9.8M
Molecular Mechanisms of Human DNA Polymerase Beta Catalysis, Fidelity and Selective InhibitionU19CA177547 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2013 to 2017
$5.5M
SV40 T Antigen Structure and Helicase MechanismsR01AI055926 · NIAID · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2004 to 2013
$4.0M
NCI NIH HHS 1U19CA105010NCI NIH HHS U19 CA105010NCI NIH HHS U19 CA177547NIAID NIH HHS R01 AI055926NIAID NIH HHS R01-AI055926
6 · The paper itself

Abstract

Detailed understanding of the action of biological molecular machines must overcome the challenge of gaining a clear knowledge of the corresponding free-energy landscape. An example for this is the elucidation of the nature of converting chemical energy to torque and work in the rotary molecular motor of F1-ATPase. A major part of the challenge involves understanding the rotary-chemical coupling from a non-phenomenological structure/energy description. Here we focused on using a coarse-grained model of F1-ATPase to generate a structure-based free-energy landscape of the rotary-chemical process of the whole system. In particular, we concentrated on exploring the possible impact of the position of the catalytic dwell on the efficiency and torque generation of the molecular machine. It was found that the experimentally observed torque can be reproduced with landscapes that have different positions for the catalytic dwell on the rotary-chemical surface. Thus, although the catalysis is undeniably required for torque generation, the experimentally observed position of the catalytic dwell at 80° might not have a clear advantage for the force generation by F1-ATPase. This further implies that the rotary-chemical couplings in these biological motors are quite robust and their efficiencies do not depend explicitly on the position of the catalytic dwells. Rather, the specific positioning of the dwells with respect to the rotational angle is a characteristic arising due to the structural construct of the molecular machine and might not bear any clear connection to the thermodynamic efficiency for the system.

Indexed as

Adenosine TriphosphateBacterial ProteinsBiophysical PhenomenaCatalysisHydrolysisMolecular Motor ProteinsProtein ConformationProton-Translocating ATPasesRotationTemperatureThermodynamicsTorqueAdenosine TriphosphateBacterial ProteinsMolecular Motor ProteinsProton-Translocating ATPasesbioenergeticsconformational surfaceF0F1-ATP synthaserotary-chemical surface

Identifiers

PMID26537397
PMCPMC4873004
OpenAlexW2124120289

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.