Evidence map›Paper›PMID 27682113›Full record

ArticleMicroorganisms2015

Sulfur Oxygenase Reductase (Sor) in the Moderately Thermoacidophilic Leaching Bacteria: Studies in Sulfobacillus thermosulfidooxidans and Acidithiobacillus caldus.

Claudia Janosch, Francisco Remonsellez, Wolfgang Sand, Mario Vera

Open access · goldAbstract read
In one paragraph

Article in Microorganisms, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Transcriptomic Analysis of the StrainInternational journal of molecular sciences · 2025
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  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Persulfide Dioxygenase FromFrontiers in microbiology · 2018
    Article
  13. Weak Iron Oxidation byFrontiers in microbiology · 2018
    Article
  14. Article
  15. Sulfur Oxidation in the Acidophilic AutotrophicFrontiers in microbiology · 2018
    Review
  16. 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

4 authors at 2 institutions in 2 countries.

Claudia JanoschBiofilm Centre, Aquatische Biotechnologie, Universität Duisburg-Essen, Universitätstraße 5, Essen, 45141, Germany. claudia.janosch@gmx.de.
Francisco RemonsellezLaboratorio de Tecnología de Membranas, Biotecnología y Medio Ambiente, Departamento de Ingeniería Química, Universidad Católica del Norte, Antofagasta 1270709, Chile. fremonse@ucn.cl.
Wolfgang SandBiofilm Centre, Aquatische Biotechnologie, Universität Duisburg-Essen, Universitätstraße 5, Essen, 45141, Germany. wolfgang.sand@uni-due.de.
Mario VeraBiofilm Centre, Aquatische Biotechnologie, Universität Duisburg-Essen, Universitätstraße 5, Essen, 45141, Germany. mario.vera@uni-due.de.
University of Duisburg-Essen · DEUniversidad Católica del Norte · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sulfur oxygenase reductase (Sor) catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide. Being considered an "archaeal like" enzyme, it is also encoded in the genomes of some acidophilic leaching bacteria such as Acidithiobacillus caldus, Acidithiobacillus thiooxidans, Acidithiobacillus ferrivorans and Sulfobacillus thermosulfidooxidans, among others. We measured Sor activity in crude extracts from Sb. thermosulfidooxidans DSM 9293(T). The optimum temperature for its oxygenase activity was achieved at 75 °C, confirming the "thermophilic" nature of this enzyme. Additionally, a search for genes probably involved in sulfur metabolism in the genome sequence of Sb. thermosulfidooxidans DSM 9293(T) was done. Interestingly, no sox genes were found. Two sor genes, a complete heterodisulfidereductase (hdr) gene cluster, three tetrathionate hydrolase (tth) genes, three sulfide quinonereductase (sqr), as well as the doxD component of a thiosulfate quinonereductase (tqo) were found. Seven At. caldus strains were tested for Sor activity, which was not detected in any of them. We provide evidence that an earlier reported Sor activity from At. caldus S1 and S2 strains most likely was due to the presence of a Sulfobacillus contaminant.

Indexed as

Acidithiobacillus caldusgenomeSulfobacillus thermosulfidooxidanssulfur metabolismsulfur oxygenase reductase

Identifiers

PMID27682113
PMCPMC5023260
OpenAlexW1780138299

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.