Evidence map›Paper›PMID 21498650›Full record

ArticleJournal of bacteriology2011

Tungsten and molybdenum regulation of formate dehydrogenase expression in Desulfovibrio vulgaris Hildenborough.

Sofia M da Silva, Catarina Pimentel, Filipa M A Valente, Claudina Rodrigues-Pousada, Inês A C Pereira

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.

  1. Pooled it
  2. Semiartificial COChemical reviews · 2026
    Review
  3. Article
  4. Review
  5. Tungsten is utilized for lactate consumption and SCFA production by a dominant human gut microbeProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Direct Biocatalytic Processes for COMolecules (Basel, Switzerland) · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. Enzymes for Efficient COThe protein journal · 2021
    Review
  12. Protein Engineering of the Soluble Metal-dependent Formate Dehydrogenase from Escherichia coli.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Molybdenum and tungsten-dependent formate dehydrogenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Review
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Sofia M da SilvaInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Catarina Pimentel
Filipa M A Valente
Claudina Rodrigues-Pousada
Inês A C Pereira
Universidade Nova de Lisboa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Formate is an important energy substrate for sulfate-reducing bacteria in natural environments, and both molybdenum- and tungsten-containing formate dehydrogenases have been reported in these organisms. In this work, we studied the effect of both metals on the levels of the three formate dehydrogenases encoded in the genome of Desulfovibrio vulgaris Hildenborough, with lactate, formate, or hydrogen as electron donors. Using Western blot analysis, quantitative real-time PCR, activity-stained gels, and protein purification, we show that a metal-dependent regulatory mechanism is present, resulting in the dimeric FdhAB protein being the main enzyme present in cells grown in the presence of tungsten and the trimeric FdhABC₃ protein being the main enzyme in cells grown in the presence of molybdenum. The putatively membrane-associated formate dehydrogenase is detected only at low levels after growth with tungsten. Purification of the three enzymes and metal analysis shows that FdhABC₃ specifically incorporates Mo, whereas FdhAB can incorporate both metals. The FdhAB enzyme has a much higher catalytic efficiency than the other two. Since sulfate reducers are likely to experience high sulfide concentrations that may result in low Mo bioavailability, the ability to use W is likely to constitute a selective advantage.

Indexed as

Bacterial ProteinsDesulfovibrio vulgarisFormate DehydrogenasesFormatesGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicMolybdenumReverse Transcriptase Polymerase Chain ReactionRNA, BacterialRNA, MessengerTungstenBacterial ProteinsFormate DehydrogenasesFormatesformic acidMolybdenumRNA, BacterialRNA, MessengerTungsten

Identifiers

PMID21498650
PMCPMC3133204
OpenAlexW2073847837

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.