Evidence map›Paper›PMID 33064490›Full record

ArticleThe journal of physical chemistry. B2020

Role of Protein Motions in Catalysis by Formate Dehydrogenase.

Dimitri Antoniou, Steven D Schwartz

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Semiartificial COChemical reviews · 2026
    Review
  2. Article
  3. Review
  4. Perspective: Path Sampling Methods Applied to Enzymatic Catalysis.Journal of chemical theory and computation · 2022
    Review
  5. Article
  6. 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

2 authors at 1 institution in 1 country.

Dimitri AntoniouDepartment of Chemistry and Biochemistry, University of Arizona, 1306 East University Blvd., Tucson, Arizona 85721, United States.
Steven D SchwartzDepartment of Chemistry and Biochemistry, University of Arizona, 1306 East University Blvd., Tucson, Arizona 85721, United States.ORCID 0000-0002-0308-1059
University of Arizona · US

Funding

Proton Transfer Dynamics in Heme-Copper OxidasesP01GM068036 · NIGMS · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI CALLENDER, ROBERT · 2004 to 2018
$26.4M
Rapid protein dynamics and catalysis: modulation by laboratory evolution, designed mutation, and protein control of electric field environmentR01GM127594 · NIGMS · UNIVERSITY OF ARIZONA · PI SCHWARTZ, STEVEN D · 2019 to 2022
$1.4M
NIGMS NIH HHS P01 GM068036NIGMS NIH HHS R01 GM127594
6 · The paper itself

Abstract

We have analyzed the reaction catalyzed by formate dehydrogenase using transition path sampling. This system has recently received experimental attention using infrared spectroscopy and heavy-enzyme studies. Some of the experimental results point to the possible importance of protein motions that are coupled to the chemical step. We found that the residue Val123 that lies behind the nicotinamide ring occasionally comes into van der Waals contact with the acceptor and that in all reactive trajectories, the barrier-crossing event is preceded by this contact, meaning that the motion of Val123 is part of the reaction coordinate. Experimental results have been interpreted with a two-dimensional formula for the chemical rate, which cannot capture effects such as the one we describe.

Indexed as

Formate DehydrogenasesProteinsCatalysisKineticsMotionFormate DehydrogenasesProteins

Identifiers

PMID33064490
PMCPMC7697370
OpenAlexW3093185213

What OpenQuestion holds

Textmetadata
LicenceTDM
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.