Evidence map›Paper›PMID 34767349›Full record

ArticleInorganic chemistry2021

Carbon Monoxide Binding to the Iron-Molybdenum Cofactor of Nitrogenase: a Detailed Quantum Mechanics/Molecular Mechanics Investigation.

Nico Spiller, Ragnar Bjornsson, Serena DeBeer, Frank Neese

Abstract read
In one paragraph

Article in Inorganic chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The HD Reaction of Nitrogenase: a Detailed Mechanism.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  10. Article
  11. Article
  12. 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.

Nico SpillerMax-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany.ORCID https://orcid.org/0000-0002-6293-4867
Ragnar BjornssonMax Planck Institute for Chemical Energy Conversion, Stiftstr 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID https://orcid.org/0000-0003-2167-8374
Serena DeBeerMax Planck Institute for Chemical Energy Conversion, Stiftstr 34-36, 45470 Mülheim an der Ruhr, Germany.ORCID https://orcid.org/0000-0002-5196-3400
Frank NeeseMax-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany.ORCID https://orcid.org/0000-0003-4691-0547

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbon monoxide (CO) is a well-known inhibitor of nitrogenase activity. Under turnover conditions, CO binds to FeMoco, the active site of Mo nitrogenase. Time-resolved IR measurements suggest an initial terminal CO at 1904 cm

Indexed as

Quantum TheoryBinding SitesCarbon MonoxideCrystallography, X-RayModels, MolecularMolybdoferredoxinNitrogenaseCarbon MonoxideMolybdoferredoxinNitrogenase

Identifiers

PMID34767349
PMCPMC8653219

What OpenQuestion holds

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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.