Evidence map›Paper›PMID 25476858›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2015

Molybdenum and tungsten-dependent formate dehydrogenases.

Luisa B Maia, José J G Moura, Isabel Moura

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

54 citing papers in PubMed, 151 citations in OpenAlex.

  1. One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Semiartificial COChemical reviews · 2026
    Review
  6. Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. 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
  12. Article
  13. Insights into periplasmic nitrate reductase function under single turnover.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  14. The energy metabolism ofApplied and environmental microbiology · 2024
    Article
  15. Article
  16. Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Luisa B MaiaUCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal, luisa.maia@fct.unl.pt.
José J G Moura
Isabel Moura
Universidade Nova de Lisboa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The prokaryotic formate metabolism is considerably diversified. Prokaryotes use formate in the C1 metabolism, but also evolved to exploit the low reduction potential of formate to derive energy, by coupling its oxidation to the reduction of numerous electron acceptors. To fulfil these varied physiological roles, different types of formate dehydrogenase (FDH) enzymes have evolved to catalyse the reversible 2-electron oxidation of formate to carbon dioxide. This review will highlight our present knowledge about the diverse physiological roles of FDH in prokaryotes, their modular structural organisation and active site structures and the mechanistic strategies followed to accomplish the formate oxidation. In addition, the ability of FDH to catalyse the reverse reaction of carbon dioxide reduction, a potentially relevant reaction for carbon dioxide sequestration, will also be addressed.

Indexed as

Energy MetabolismCarbon DioxideFormate DehydrogenasesFormatesMolybdenumProkaryotic CellsTungstenCarbon DioxideFormate DehydrogenasesFormatesformic acidMolybdenumTungsten

Identifiers

PMID25476858
OpenAlexW2067606391

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.