Evidence map›Paper›PMID 39261000›Full record

ArticleMethods in enzymology2024

Spectroscopic definition of ferrous active sites in non-heme iron enzymes.

Edward I Solomon, Robert R Gipson

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in enzymology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Insights into the pH-dependent reactivity and substrate induced active-site reorganization of the non- heme iron enzyme CthEgtB.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  2. 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

2 authors.

Edward I SolomonDepartment of Chemistry, Stanford University, Stanford, CA, United States; Stanford Synchrotron Radiation Lightsource, SLAC National Acceleration Laboratory, Stanford University, Menlo Park, CA, United States. Electronic address: edward.solomon@stanford.edu.
Robert R GipsonDepartment of Chemistry, Stanford University, Stanford, CA, United States.

Funding

Spectroscopic Characterization of Oxygen Intermediates in Non-heme and Heme Iron EnzymesR35GM145202 · NIGMS · STANFORD UNIVERSITY · PI EDWARD I SOLOMON · 2022 to 2026
$2.0M
NIGMS NIH HHS R35 GM145202
6 · The paper itself

Abstract

Non-heme iron enzymes play key roles in antibiotic, neurotransmitter, and natural product biosynthesis, DNA repair, hypoxia regulation, and disease states. These enzymes had been refractory to traditional bioinorganic spectroscopic methods. Thus, we developed variable-temperature variable-field magnetic circular dichroism (VTVH MCD) spectroscopy to experimentally define the excited and ground ligand field states of non-heme ferrous enzymes (Solomon et al., 1995). This method provides detailed geometric and electronic structure insight and thus enables a molecular level understanding of catalytic mechanisms. Application of this method across the five classes of non-heme ferrous enzymes has defined that a general mechanistic strategy is utilized where O

Indexed as

Catalytic DomainCircular DichroismFerrous CompoundsIronNonheme Iron ProteinsOxygenFerrous CompoundsIronNonheme Iron ProteinsOxygenFerrous enzyme mechanismsLigand field theoryMagnetic circular dichroism spectroscopyNon-heme iron enzymesNon-Kramers’ ionsSaturation magnetization

Identifiers

PMID39261000
PMCPMC11391101

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.