Evidence map›Paper›PMID 24561181›Full record

ArticleBiochemical pharmacology2014

Mammalian flavin-containing monooxygenase (FMO) as a source of hydrogen peroxide.

Lisbeth K Siddens, Sharon K Krueger, Marilyn C Henderson, David E Williams

Open access · greenAbstract read
In one paragraph

Article in Biochemical pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
9.0field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. snRNA-seq identifies Fmo2npj metabolic health and disease · 2026
    Article
  4. Article
  5. Article
  6. Flavin-dependent enzymatic and photochemical interconversions between phenylarsonic and phenylarsonous acids.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
    Article
  7. Article
  8. Flavin-containing monooxygenase (FMO): Beyond xenobiotics.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
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  10. Article
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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

4 authors at 2 institutions in 1 country.

Lisbeth K SiddensDepartment of Environmental and Molecular Toxicology, USA. Electronic address: siddensb@onid.oregonstate.edu.
Sharon K KruegerThe Linus Pauling Institute, Oregon State University, Corvallis, OR 97331, USA. Electronic address: sharon.krueger@oregonstate.edu.
Marilyn C HendersonDepartment of Environmental and Molecular Toxicology, USA. Electronic address: marilyn.henderson@comcast.net.
David E WilliamsDepartment of Environmental and Molecular Toxicology, USA; The Linus Pauling Institute, Oregon State University, Corvallis, OR 97331, USA. Electronic address: david.williams@oregonstate.edu.
Oregon State University · USSociety of Environmental Toxicology and Chemistry · US

Funding

Reducing Susceptibility to Environmental Stress Throughout the Life SpanP30ES000210 · NIEHS · OREGON STATE UNIVERSITY · PI BECKMAN, JOSEPH S · 1985 to 2015
$21.4M
FLAVIN-CONTAINING MONOOXYGENASES IN LUNGR01HL038650 · NHLBI · OREGON STATE UNIVERSITY · PI WILLIAMS, DAVID E · 1992 to 2013
$3.5M
NOVEL FAD-CONTAINING MONOOXYGENASE IN LUNGR29HL038650 · NHLBI · OREGON STATE UNIVERSITY · PI WILLIAMS, DAVID E. · 1987 to 1991
–
NHLBI NIH HHS HL038650NHLBI NIH HHS R01 HL038650NIEHS NIH HHS P30 ES000210
6 · The paper itself

Abstract

Flavin-containing monooxygenase (FMO) oxygenates drugs/xenobiotics containing a soft nucleophile through a C4a hydroperoxy-FAD intermediate. Human FMOs 1, 2 and 3, expressed in Sf9 insect microsomes, released 30-50% of O₂ consumed as H₂O₂ upon addition of NADPH. Addition of substrate had little effect on H₂O₂ production. Two common FMO2 (the major isoform in the lung) genetic polymorphisms, S195L and N413K, were examined for generation of H₂O₂. FMO2 S195L exhibited higher "leakage", producing much greater amounts of H₂O₂, than ancestral FMO2 (FMO2.1) or the N413K variant. S195L was distinct in that H₂O₂ generation was much higher in the absence of substrate. Addition of superoxide dismutase did not impact H₂O₂ release. Catalase did not reduce levels of H₂O₂ with either FMO2.1 or FMO3 but inhibited H₂O₂ generated by FMO2 allelic variants N413K and S195L. These data are consistent with FMO molecular models. S195L resides in the GxGxSG/A NADP(+) binding motif, in which serine is highly conserved (76/89 known FMOs). We hypothesize that FMO, especially allelic variants such as FMO2 S195L, may enhance the toxicity of xenobiotics such as thioureas/thiocarbamides both by generation of sulfenic and sulfinic acid metabolites and enhanced release of reactive oxygen species (ROS) in the form of H₂O₂.

Indexed as

AnimalsHumansHydrogen PeroxideOxygenasesSf9 Cellsdimethylaniline monooxygenase (N-oxide forming)Hydrogen PeroxideOxygenasesFlavin-containing monooxygenaseGenetic polymorphismHydrogen peroxideOxidative stressPulmonary FMO2

Identifiers

PMID24561181
PMCPMC4116332
OpenAlexW1997115553

What OpenQuestion holds

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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.