Evidence map›Paper›PMID 20582160›Full record

ArticleJournal of physical organic chemistry2010

On the Origin of the Chemical Barrier and Tunneling in Enzymes.

Sara Quaytman Machleder, Exequiel T Pineda, Steven D Schwartz

Abstract read
In one paragraph

Article in Journal of physical organic chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Computational Studies of Catalytic Loop Dynamics inThe journal of physical chemistry. B · 2019
    Article
  2. Article
  3. Carbon Acidity in Enzyme Active Sites.Frontiers in bioengineering and biotechnology · 2019
    Article
  4. Review
  5. Dynamics and dissipation in enzyme catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  6. Article
  7. 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

3 authors.

Sara Quaytman MachlederDept. of Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bx, NY 10461.
Exequiel T Pineda
Steven D Schwartz

Funding

Proton Transfer Dynamics in Heme-Copper OxidasesP01GM068036 · NIGMS · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI CALLENDER, ROBERT · 2004 to 2018
$26.4M
NIGMS NIH HHS P01 GM068036
6 · The paper itself

Abstract

This paper presents both a review of some recent results from our group and experimental groups, and some new theoretical results all of which are helping to form a more physically rigorous picture of the process of enzymatic catalysis. A common classical picture of enzymatic catalysis is the transition state tight binding model. Schwartz and Schramm1 have recently argued from both theoretical and experimental results that this picture is incorrect. We now investigate what the nature of barriers might be in enzymatic reactions, and what this viewpoint might imply for tunneling in a hydrogen transfer enzyme. For lactate dehydrogenase we conclude that the enzymes role in catalysis is at least partially to hunt through configuration space for those configurations that minimize chemical free energy barriers. Those configurations do not seem to be stable basins on the free energy surface, and in fact the overall free energy barrier to reaction may well largely be due to this stochastic hunt - both probabilistically and energetically. We suggest further computations to test this hypothesis.

Identifiers

PMID20582160
PMCPMC2889710

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Registered trials

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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.