Evidence map›Paper›PMID 25425163›Full record

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

Electronic structure contributions to reactivity in xanthine oxidase family enzymes.

Benjamin W Stein, Martin L Kirk

Open access · greenAbstract 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 34 citations in OpenAlex.

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  8. Structural, Mechanistic, and Functional Insights into anMolecules (Basel, Switzerland) · 2021
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  14. A realistic in silico model for structure/function studies of molybdenum-copper CO dehydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    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

2 authors at 1 institution in 1 country.

Benjamin W SteinDepartment of Chemistry and Chemical Biology, University of New Mexico, MSC03 2060, 300 Terrace St. NE, Albuquerque, NM, 87131, USA.
Martin L Kirk
University of New Mexico · US

Funding

Spectroscopic Studies of Molybdoenzymes & ModelsR01GM057378 · NIGMS · UNIVERSITY OF NEW MEXICO · PI MARTIN L KIRK · 1998 to 2026
$6.9M
NIGMS NIH HHS GM-057378NIGMS NIH HHS R01 GM057378
6 · The paper itself

Abstract

We review the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes with a specific emphasis on electronic structure contributions to reactivity. In addition to xanthine and aldehyde oxidoreductases, which catalyze the two-electron oxidation of aromatic heterocycles and aldehyde substrates, this mini-review highlights recent work on the closely related carbon monoxide dehydrogenase (CODH) that catalyzes the oxidation of CO using a unique Mo-Cu heterobimetallic active site. A primary focus of this mini-review relates to how spectroscopy and computational methods have been used to develop an understanding of critical relationships between geometric structure, electronic structure, and catalytic function.

Indexed as

ElectronsAldehyde OxidoreductasesCatalysisCrystallography, X-RayElectron Spin Resonance SpectroscopyModels, MolecularMolybdenumMultienzyme ComplexesOxidation-ReductionProtein ConformationXanthineXanthine OxidaseAldehyde Oxidoreductasescarbon monoxide dehydrogenaseMolybdenumMultienzyme ComplexesXanthineXanthine Oxidase

Identifiers

PMID25425163
PMCPMC4867223
OpenAlexW2012476277

What OpenQuestion holds

Textmetadata
LicenceTDM
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.