Evidence map›Paper›PMID 27190141›Full record

ArticleFEMS microbiology letters2016

A sulfide:quinone oxidoreductase from Chlorobaculum tepidum displays unusual kinetic properties.

Kevin E Shuman, Thomas E Hanson

Open access · bronzeAbstract read
In one paragraph

Article in FEMS microbiology letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed, 20 citations in OpenAlex.

  1. Applied and environmental microbiology · 2025
    Article
  2. Quinone binding site in a type VI sulfide:quinone oxidoreductase.Applied microbiology and biotechnology · 2022
    Article
  3. Article
  4. Cross-talk of MicroRNA and hydrogen sulfide: A novel therapeutic approach for bone diseases.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2017
    Review
  5. 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 2 institutions in 1 country.

Kevin E ShumanDepartment of Biological Sciences, University of Delaware, Newark, DE 19711, USA Delaware Biotechnology Institute, University of Delaware, Newark, DE 19711, USA.
Thomas E HansonDepartment of Biological Sciences, University of Delaware, Newark, DE 19711, USA Delaware Biotechnology Institute, University of Delaware, Newark, DE 19711, USA School of Marine Science and Policy, University of Delaware, Newark, DE 19711, USA tehanson@udel.edu.
Biotechnology Institute · USUniversity of Delaware · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sulfide:quinone oxidoreductase (SQR) is the primary sulfide-oxidizing enzyme found in all three domains of life. Of the six phylogenetically distinct types of SQR, four have representatives that have been biochemically characterized. The genome of Chlorobaculum tepidum encodes three SQR homologs. One of these, encoded by CT1087, is a type VI SQR that has been previously shown to be required for growth at high sulfide concentrations and to be expressed in sulfide-dependent manner. Therefore, CT1087 was hypothesized to be a high sulfide adapted SQR. CT1087 was expressed in Escherichia coli with an N-terminal His-tag (CT1087NHis6) and purified by Ni-NTA chromatography. CT1087NHis6 was active and contained FAD as a strongly bound cofactor. The measured kinetic parameters for CT1087NHis6 indicate a low affinity for sulfide and a high enzymatic turnover rate consistent with the hypothesis for its function inferred from genetic and expression data. These are the first kinetic data for a type VI SQR and have implications for structure-function analyses of all SQR's.

Indexed as

ChlorobiEnergy MetabolismEscherichia coliFlavin-Adenine DinucleotideKineticsNAD(P)H Dehydrogenase (Quinone)PhylogenySulfidesFlavin-Adenine DinucleotideNAD(P)H Dehydrogenase (Quinone)SulfidesChlorobaculum tepidumenergy metabolismsulfide:quinone oxidoreductaseSulfur2016sulfur metabolism

Identifiers

PMID27190141
PMCPMC5975255
OpenAlexW2339008861

What OpenQuestion holds

Textmetadata
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.