Evidence map›Paper›PMID 28635274›Full record

ArticleJournal of the American Chemical Society2017

Oxidation-State-Dependent Binding Properties of the Active Site in a Mo-Containing Formate Dehydrogenase.

William E Robinson, Arnau Bassegoda, Erwin Reisner, Judy Hirst

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 91 citations in OpenAlex.

  1. Pooled it
  2. Semiartificial COChemical reviews · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Solar-Driven Paired COJournal of the American Chemical Society · 2025
    Article
  7. All-in-One COAccounts of chemical research · 2024
    Review
  8. Article
  9. A synergetic cocatalyst for conversion of carbon dioxide, sunlight, and water into methanol.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Connecting Biological and Synthetic Approaches for Electrocatalytic COAngewandte Chemie (International ed. in English) · 2024
    Review
  11. Direct Biocatalytic Processes for COMolecules (Basel, Switzerland) · 2023
    Review
  12. Metal-Containing Formate Dehydrogenases, a Personal View.Molecules (Basel, Switzerland) · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Understanding the local chemical environment of bioelectrocatalysis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  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

4 authors at 2 institutions in 1 country.

William E RobinsonDepartment of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, U.K.
Arnau BassegodaMedical Research Council Mitochondrial Biology Unit, University of Cambridge , Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, U.K.
Erwin ReisnerDepartment of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, U.K.ORCID 0000-0002-7781-1616
Judy HirstMedical Research Council Mitochondrial Biology Unit, University of Cambridge , Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, U.K.ORCID 0000-0001-8667-6797
MRC Mitochondrial Biology Unit · GBUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I026367/1Biotechnology and Biological Sciences Research Council BB/J000124/1Medical Research Council MC_U105663141Medical Research Council MC_UU_00015/2Medical Research Council MC_UU_00015/7Medical Research Council U105663141
6 · The paper itself

Abstract

Molybdenum-containing formate dehydrogenase H from Escherichia coli (EcFDH-H) is a powerful model system for studies of the reversible reduction of CO

Indexed as

Binding SitesCarbon DioxideCatalytic DomainCoordination ComplexesEscherichia coliFormate DehydrogenasesFormatesMolybdenumOxidation-ReductionCarbon DioxideCoordination ComplexesFormate DehydrogenasesFormatesMolybdenum

Identifiers

PMID28635274
PMCPMC5532686
OpenAlexW2675006404

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.