Evidence map›Paper›PMID 25549604›Full record

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

The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry.

Ragnar Bjornsson, Frank Neese, Richard R Schrock, Oliver Einsle, Serena DeBeer

Open access · hybridAbstract readReview
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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 83 citations in OpenAlex.

  1. Biomimetic [MFeInorganic chemistry · 2025
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  10. Structural insight into [Fe-SChemical science · 2020
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  17. Some nontoxic metal-based drugs for selected prevalent tropical pathogenic diseases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Review
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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

5 authors at 5 institutions in 3 countries.

Ragnar BjornssonMax-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany, ragnarbj@hi.is.
Frank Neese
Richard R Schrock
Oliver Einsle
Serena DeBeer
Cornell University · USMassachusetts Institute of Technology · USMax Planck Institute for Chemical Energy Conversion · DEUniversity of Freiburg · DEUniversity of Iceland · IS

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological nitrogen fixation is enabled by molybdenum-dependent nitrogenase enzymes, which effect the reduction of dinitrogen to ammonia using an Fe7MoS9C active site, referred to as the iron molybdenum cofactor or FeMoco. In this mini-review, we summarize the current understanding of the molecular and electronic structure of FeMoco. The advances in our understanding of the active site structure are placed in context with the parallel evolution of synthetic model studies. The recent discovery of Mo(III) in the FeMoco active site is highlighted with an emphasis placed on the important role that model studies have played in this finding. In addition, the reactivities of synthetic models are discussed in terms of their relevance to the enzymatic system.

Indexed as

Nitrogen FixationProtein ConformationApoproteinsCatalysisCatalytic DomainCrystallography, X-RayIronModels, MolecularMolybdenumMolybdoferredoxinApoproteinsIronMolybdenumMolybdoferredoxinnitrogenase apomolybdenum-iron protein, Bacteria

Identifiers

PMID25549604
PMCPMC4334110
OpenAlexW2088927038

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.