Evidence map›Paper›PMID 36235278›Full record

ReviewMolecules (Basel, Switzerland)2022

Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly.

Markus W Ribbe, Kamil Górecki, Mario Grosch, Joseph B Solomon, Robert Quechol, Yiling A Liu, Chi Chung Lee, Yilin Hu

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Molecules (Basel, Switzerland), 2022. 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
0.5field-weighted citation impact, top 46% 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. 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

8 authors at 1 institution in 1 country.

Markus W RibbeDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Kamil GóreckiDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.ORCID 0000-0002-9672-2408
Mario GroschDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Joseph B SolomonDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Robert QuecholDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Yiling A LiuDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.ORCID 0000-0003-4154-2888
Chi Chung LeeDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Yilin HuDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
University of California, Irvine · US

Funding

Nitrogenase Assembly MechanismR01GM067626 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI RIBBE, MARKUS W · 2003 to 2024
$6.3M
T32 for Training in Microbiology & Infectious DiseasesT32AI141346 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI Celia Goulding, Melissa Bruckner Lodoen · 2019 to 2026
$1.0M
National Science Foundation CHE-1651398NIAID NIH HHS T32 AI141346NIGMS NIH HHS R01 GM067626NIH HHS GM67626
6 · The paper itself

Abstract

The Fe protein of nitrogenase plays multiple roles in substrate reduction and metallocluster assembly. Best known for its function to transfer electrons to its catalytic partner during nitrogenase catalysis, the Fe protein is also a key player in the biosynthesis of the complex metalloclusters of nitrogenase. In addition, it can function as a reductase on its own and affect the ambient reduction of CO

Indexed as

Carbon DioxideNitrogenaseHydrocarbonsOxidation-ReductionOxidoreductasesCarbon DioxideHydrocarbonsNitrogenasenitrogenase reductaseOxidoreductasesbiosynthesisC1 substrate reductioncatalysisFe proteinFeS enzymenitrogenasereductase

Identifiers

PMID36235278
PMCPMC9571451
OpenAlexW4303981340

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.