Evidence map›Paper›PMID 23361122›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013

Gaining insight into the chemistry of lipoxygenases: a computational investigation into the catalytic mechanism of (8R)-lipoxygenase.

Eric A C Bushnell, Riam Jamil, James W Gauld

Abstract read
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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
  2. EPR Spectroscopic Studies of Lipoxygenases.Chemistry, an Asian journal · 2020
    Review
  3. Mono- and binuclear non-heme iron chemistry from a theoretical perspective.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Review
  4. The structural basis for specificity in lipoxygenase catalysis.Protein science : a publication of the Protein Society · 2015
    Review
  5. Article
  6. Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    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

3 authors at 1 institution in 1 country.

Eric A C BushnellDepartment of Chemistry and Biochemistry, University of Windsor, Windsor, ON, N9B 3P4, Canada.
Riam Jamil
James W Gauld
University of Windsor · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipoxygenases (LOXs) are ubiquitous in nature and catalyze a range of life-essential reactions within organisms. In particular they are critical to the formation of eicosanoids, which are critical for normal cell function. However, a number of important questions about the reactivity and mechanism of these enzymes still remain. Specifically, although the initial step in the mechanism of LOXs has been well studied, little is known of subsequent steps. Thus, with use of a quantum mechanical/molecular mechanical approach, the complete catalytic mechanism of (8R)-LOX was investigated. The results have provided a better understanding of the general chemistry of LOXs as a whole. In particular, from comparisons with soybean LOX-1, it appears that the initial proton-coupled electron transfer may be very similar among all LOXs. Furthermore, LOXs appear to undergo multistate reactivity where potential spin inversion of an electron may occur either in the attack of O(2) or in the regeneration of the active site. Lastly, it is shown that with the explicit modeling of the environment, the regeneration of the active center likely occurs via the rotation of the intermediate followed by an outer-sphere [Formula: see text] transfer as opposed to the formation of a "purple intermediate" complex.

Indexed as

AnimalsAnthozoaArachidonate LipoxygenasesCatalytic DomainEnzyme ActivationGlycine maxLipoxygenaseMolecular Docking SimulationPeroxidesProtein ConformationQuantum TheoryArachidonate LipoxygenasesLipoxygenaseperhydroxyl radicalPeroxides

Identifiers

PMID23361122
OpenAlexW2074462166

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.