Evidence map›Paper›PMID 36173876›Full record

ArticleJournal of the American Chemical Society2022

Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insights into the Mechanism of Oxidative Catalysis.

Leon P Jenner, Jason C Crack, Julia M Kurth, Zuzana Soldánová, Linda Brandt, Katarzyna P Sokol, Erwin Reisner, Justin M Bradley, Christiane Dahl, Myles R Cheesman and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. ZoonoticEmerging microbes & infections · 2026
    Article
  2. 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

11 authors at 3 institutions in 2 countries.

Leon P JennerCentre for Molecular and Structural Biochemistry, School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich Research Park, NorwichNR4 7TJ, United Kingdom.ORCID 0000-0002-9657-4783
Jason C CrackCentre for Molecular and Structural Biochemistry, School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich Research Park, NorwichNR4 7TJ, United Kingdom.ORCID 0000-0002-4979-1910
Julia M KurthInstitut für Mikrobiologie & Biotechnologie, Friedrich Wilhelms Universität Bonn, D-53115Bonn, Germany.
Zuzana SoldánováCentre for Molecular and Structural Biochemistry, School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich Research Park, NorwichNR4 7TJ, United Kingdom.
Linda BrandtInstitut für Mikrobiologie & Biotechnologie, Friedrich Wilhelms Universität Bonn, D-53115Bonn, Germany.
Katarzyna P SokolYusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, CambridgeCB2 1EW, United Kingdom.
Erwin ReisnerYusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, CambridgeCB2 1EW, United Kingdom.ORCID 0000-0002-7781-1616
Justin M BradleyCentre for Molecular and Structural Biochemistry, School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich Research Park, NorwichNR4 7TJ, United Kingdom.
Christiane DahlInstitut für Mikrobiologie & Biotechnologie, Friedrich Wilhelms Universität Bonn, D-53115Bonn, Germany.ORCID 0000-0001-8288-7546
Myles R CheesmanCentre for Molecular and Structural Biochemistry, School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich Research Park, NorwichNR4 7TJ, United Kingdom.
Julea N ButtCentre for Molecular and Structural Biochemistry, School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich Research Park, NorwichNR4 7TJ, United Kingdom.ORCID 0000-0002-9624-5226
University of East Anglia · GBUniversity of Bonn · DEUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K009885/1Biotechnology and Biological Sciences Research Council BB/L022176/1
6 · The paper itself

Abstract

Thiosulfate dehydrogenases are bacterial cytochromes that contribute to the oxidation of inorganic sulfur. The active sites of these enzymes contain low-spin

Indexed as

CysteineHemeBacterial ProteinsCatalysisCytochromesLigandsOxidation-ReductionOxidative StressOxidoreductasesSulfitesSulfurThiosulfatesBacterial ProteinsCysteineCytochromesHemeLigandsOxidoreductasesSulfitesSulfurthiosulfate dehydrogenaseThiosulfates

Identifiers

PMID36173876
PMCPMC9562282
OpenAlexW4297995686

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.