Evidence map›Paper›PMID 25487146›Full record

ArticleNature2015

The heat released during catalytic turnover enhances the diffusion of an enzyme.

Clement Riedel, Ronen Gabizon, Christian A M Wilson, Kambiz Hamadani, Konstantinos Tsekouras, Susan Marqusee, Steve Pressé, Carlos Bustamante

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
–field-weighted citation impact
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

75 citing papers in PubMed.

  1. Review
  2. Article
  3. Enzyme Catalytic Parameters and Evolution Across the Dissipation Plane.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Clement RiedelCalifornia Institute for Quantitative Biosciences, QB3, University of California, Berkeley, California 94720, USA.
Ronen GabizonCalifornia Institute for Quantitative Biosciences, QB3, University of California, Berkeley, California 94720, USA.
Christian A M Wilson1] California Institute for Quantitative Biosciences, QB3, University of California, Berkeley, California 94720, USA [2] Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, 1058 Santiago, Chile.
Kambiz HamadaniCalifornia Institute for Quantitative Biosciences, QB3, University of California, Berkeley, California 94720, USA.
Konstantinos TsekourasDepartment of Physics, Indiana University-Purdue University Indianapolis (IUPUI), Indiana 46202, USA.
Susan Marqusee1] California Institute for Quantitative Biosciences, QB3, University of California, Berkeley, California 94720, USA [2] Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Steve Pressé1] Department of Physics, Indiana University-Purdue University Indianapolis (IUPUI), Indiana 46202, USA [2] Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Indiana 46202, USA.
Carlos Bustamante1] California Institute for Quantitative Biosciences, QB3, University of California, Berkeley, California 94720, USA [2] Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA [3] Jason L. Choy Laboratory of Single-Molecule Biophysics and Department of Physics, University of California, Berkeley, California 94720, USA [4] Department of Chemistry, University of California, Berkeley, California 94720, USA [5] Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA [6] Kavli Energy Nano Sciences Institute, University of California, Berkeley and Lawrence Berkeley National Laboratory, California 94720, USA.

Funding

The Role of the Ribosome in the Accuracy of TranslationR01GM065050 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CATE, JAMIE H · 2001 to 2022
$7.4M
Sequence and Environmental Determinants of the Protein Energy LandscapeR01GM050945 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARQUSEE, SUSAN · 1999 to 2022
$7.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01-GM0325543NIGMS NIH HHS R01 GM050945NIGMS NIH HHS R01-GM05945NIGMS NIH HHS R01 GM065050NIGMS NIH HHS R01-GM65050Wellcome Trust
6 · The paper itself

Abstract

Recent studies have shown that the diffusivity of enzymes increases in a substrate-dependent manner during catalysis. Although this observation has been reported and characterized for several different systems, the precise origin of this phenomenon is unknown. Calorimetric methods are often used to determine enthalpies from enzyme-catalysed reactions and can therefore provide important insight into their reaction mechanisms. The ensemble averages involved in traditional bulk calorimetry cannot probe the transient effects that the energy exchanged in a reaction may have on the catalyst. Here we obtain single-molecule fluorescence correlation spectroscopy data and analyse them within the framework of a stochastic theory to demonstrate a mechanistic link between the enhanced diffusion of a single enzyme molecule and the heat released in the reaction. We propose that the heat released during catalysis generates an asymmetric pressure wave that results in a differential stress at the protein-solvent interface that transiently displaces the centre-of-mass of the enzyme (chemoacoustic effect). This novel perspective on how enzymes respond to the energy released during catalysis suggests a possible effect of the heat of reaction on the structural integrity and internal degrees of freedom of the enzyme.

Indexed as

BiocatalysisDiffusionHot TemperatureAlkaline PhosphataseAnimalsCalorimetryCatalaseCatalytic DomainCattleEnzymesKineticsSaccharomyces cerevisiaeSpectrometry, FluorescenceThermodynamicsTriose-Phosphate IsomeraseUreaseAlkaline PhosphataseCatalaseEnzymesTriose-Phosphate IsomeraseUrease

Identifiers

PMID25487146
PMCPMC4363105

What OpenQuestion holds

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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.