Evidence map›Paper›PMID 28873420›Full record

ArticlePloS one2017

Discovery of a new subgroup of sulfur dioxygenases and characterization of sulfur dioxygenases in the sulfur metabolic network of Acidithiobacillus caldus.

Wei Wu, Xin Pang, Jianqiang Lin, Xiangmei Liu, Rui Wang, Jianqun Lin, Linxu Chen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. DiverseApplied and environmental microbiology · 2025
    Article
  3. Mechanism of Intracellular Elemental Sulfur Oxidation inInternational journal of molecular sciences · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. New Insights IntoFrontiers in microbiology · 2020
    Article
  14. Article
  15. Article
  16. Persulfide Dioxygenase FromFrontiers in microbiology · 2018
    Article
  17. Sulfur Oxidation in the Acidophilic AutotrophicFrontiers in microbiology · 2018
    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

7 authors at 1 institution in 1 country.

Wei WuState Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China.ORCID http://orcid.org/0000-0002-2599-924X
Xin PangState Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China.
Jianqiang LinState Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China.
Xiangmei LiuState Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China.
Rui WangState Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China.
Jianqun LinState Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China.
Linxu ChenState Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China.
Shandong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acidithiobacillus caldus is a chemolithoautotrophic sulfur-oxidizing bacterium that is widely used for bioleaching processes. Acidithiobacillus spp. are suggested to contain sulfur dioxygenases (SDOs) that facilitate sulfur oxidation. In this study, two putative sdo genes (A5904_0421 and A5904_1112) were detected in the genome of A. caldus MTH-04 by BLASTP searching with the previously identified SDO (A5904_0790). We cloned and expressed these genes, and detected the SDO activity of recombinant protein A5904_0421 by a GSH-dependent in vitro assay. Phylogenetic analysis indicated that A5904_0421and its homologous SDOs, mainly found in autotrophic bacteria, were distantly related to known SDOs and were categorized as a new subgroup of SDOs. The potential functions of genes A5904_0421 (termed sdo1) and A5904_0790 (termed sdo2) were investigated by generating three knockout mutants (Δsdo1, Δsdo2 and Δsdo1&2), two sdo overexpression strains (OE-sdo1 and OE-sdo2) and two sdo complemented strains (Δsdo1/sdo1' and Δsdo2/sdo2') of A. caldus MTH-04. Deletion or overexpression of the sdo genes did not obviously affect growth of the bacteria on S0, indicating that the SDOs did not play an essential role in the oxidation of extracellular elemental sulfur in A. caldus. The deletion of sdo1 resulted in complete inhibition of growth on tetrathionate, slight inhibition of growth on thiosulfate and increased GSH-dependent sulfur oxidation activity on S0. Transcriptional analysis revealed a strong correlation between sdo1 and the tetrathionate intermediate pathway. The deletion of sdo2 promoted bacterial growth on tetrathionate and thiosulfate, and overexpression of sdo2 altered gene expression patterns of sulfide:quinone oxidoreductase and rhodanese. Taken together, the results suggest that sdo1 is essential for the survival of A. caldus when tetrathionate is used as the sole energy resource, and sdo2 may also play a role in sulfur metabolism.

Indexed as

Metabolic Networks and PathwaysAcidithiobacillusAmino Acid SequenceDioxygenasesGene Expression Regulation, BacterialGene Knockout TechniquesGenetic Complementation TestGlutathioneHydrogen-Ion ConcentrationKineticsMutationOxidation-ReductionPhylogenyRecombinant ProteinsRNA, MessengerSequence AlignmentDioxygenasesGlutathioneRecombinant ProteinsRNA, MessengerSulfatesSulfursulfur dioxygenase

Identifiers

PMID28873420
PMCPMC5584763
OpenAlexW2752581471

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.