Evidence map›Paper›PMID 20421652›Full record

ArticleThe Journal of biological chemistry2010

Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes.

Aurélie Lieutaud, Robert van Lis, Simon Duval, Line Capowiez, Daniel Muller, Régine Lebrun, Sabrina Lignon, Marie-Laure Fardeau, Marie-Claire Lett, Wolfgang Nitschke and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

14 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. New Arsenite Oxidase Gene (Frontiers in microbiology · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. The mononuclear molybdenum enzymes.Chemical reviews · 2014
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Involvement of RpoN in regulating bacterial arsenite oxidation.Applied and environmental microbiology · 2012
    Article
  13. Article
  14. 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 4 institutions in 1 country.

Aurélie LieutaudLaboratoire de Bioénergétique et Ingénierie des Protéines UPR 9036, IFR88, CNRS, F-13402 Marseille Cedex 20, France.
Robert van Lis
Simon Duval
Line Capowiez
Daniel Muller
Régine Lebrun
Sabrina Lignon
Marie-Laure Fardeau
Marie-Claire Lett
Wolfgang Nitschke
Barbara Schoepp-Cothenet
Bioénergétique et Ingénierie des Protéines · FRCentre National de la Recherche Scientifique · FRGénétique Moléculaire Génomique Microbiologie · FRInstitut de Biologie du Développement Marseille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We characterized the aro arsenite oxidation system in the novel strain Ralstonia sp. 22, a beta-proteobacterium isolated from soil samples of the Salsigne mine in southern France. The inducible aro system consists of a heterodimeric membrane-associated enzyme reacting with a dedicated soluble cytochrome c(554). Our biochemical results suggest that the weak association of the enzyme to the membrane probably arises from a still unknown interaction partner. Analysis of the phylogeny of the aro gene cluster revealed that it results from a lateral gene transfer from a species closely related to Achromobacter sp. SY8. This constitutes the first clear cut case of such a transfer in the Aro phylogeny. The biochemical study of the enzyme demonstrates that it can accommodate in vitro various cytochromes, two of which, c(552) and c(554,) are from the parent species. Cytochrome c(552) belongs to the sox and not the aro system. Kinetic studies furthermore established that sulfite and sulfide, substrates of the sox system, are both inhibitors of Aro activity. These results reinforce the idea that sulfur and arsenic metabolism are linked.

Indexed as

Amino Acid SequenceArsenatesArsenicCytochromesDNA, BacterialDNA PrimersDNA, RibosomalElectrophoresis, Polyacrylamide GelGene AmplificationKineticsMolecular Sequence DataMolecular WeightOxidoreductasesPhylogenyProtein SubunitsRalstoniaArsenatesArsenicarsenite oxidaseCytochromesDNA, BacterialDNA PrimersDNA, RibosomalOxidoreductasesProtein Subunits

Identifiers

PMID20421652
PMCPMC2898339
OpenAlexW2054981877

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.