Evidence map›Paper›PMID 32420744›Full record

ArticleThe journal of physical chemistry letters2020

Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State.

Edward Reijerse, James A Birrell, Wolfgang Lubitz

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The journal of physical chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. A personal account on 25 years of scientific literature on [FeFe]-hydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Review
  3. 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.

Edward ReijerseMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID http://orcid.org/0000-0001-9605-4510
James A BirrellMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID http://orcid.org/0000-0002-0939-0573
Wolfgang LubitzMax-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID http://orcid.org/0000-0001-7059-5327

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The active site of [FeFe] hydrogenase features a binuclear iron cofactor Fe

Indexed as

Algal ProteinsBacterial ProteinsCarbon IsotopesCarbon MonoxideCatalytic DomainChlamydomonas reinhardtiiClostridiumCoordination ComplexesDensity Functional TheoryElectron Spin Resonance SpectroscopyEnzyme InhibitorsHydrogenaseIronIron-Sulfur ProteinsLigandsModels, ChemicalAlgal ProteinsBacterial ProteinsCarbon-13Carbon IsotopesCarbon MonoxideCoordination ComplexesEnzyme InhibitorsHydrogenaseIroniron hydrogenaseIron-Sulfur ProteinsLigands

Identifiers

PMID32420744
PMCPMC7309315

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.