Evidence map›Paper›PMID 26062463›Full record

ArticleEnvironmental science and pollution research international2016

Cytochrome c adducts with PCB quinoid metabolites.

Miao Li, Lynn M Teesch, Daryl J Murry, R Marshal Pope, Yalan Li, Larry W Robertson, Gabriele Ludewig

Abstract read
In one paragraph

Article in Environmental science and pollution research international, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 48% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. 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

7 authors at 1 institution in 1 country.

Miao LiInterdisciplinary Graduate Program in Human Toxicology, Graduate College, The University of Iowa, Iowa City, IA, USA.
Lynn M TeeschHigh Resolution Mass Spectrometry Facility, The University of Iowa, Iowa City, IA, USA.
Daryl J MurryInterdisciplinary Graduate Program in Human Toxicology, Graduate College, The University of Iowa, Iowa City, IA, USA.
R Marshal PopeProteomics Facility, The University of Iowa, Iowa City, IA, USA.
Yalan LiProteomics Facility, The University of Iowa, Iowa City, IA, USA.
Larry W RobertsonInterdisciplinary Graduate Program in Human Toxicology, Graduate College, The University of Iowa, Iowa City, IA, USA.
Gabriele LudewigInterdisciplinary Graduate Program in Human Toxicology, Graduate College, The University of Iowa, Iowa City, IA, USA. gabriele-ludewig@uiowa.edu.
University of Iowa · US

Funding

Training CoreP42ES013661 · NIEHS · UNIVERSITY OF IOWA · PI HANS-JOACHIM LEHMLER · 2006 to 2026
$60.3M
Pulmonary Toxicology Facility CoreP30ES005605 · NIEHS · UNIVERSITY OF IOWA · PI Brandi Janssen · 1990 to 2026
$40.5M
NIEHS NIH HHS P30 ES005605NIEHS NIH HHS P42 ES013661
6 · The paper itself

Abstract

Polychlorinated biphenyls (PCBs) are a group of 209 individual congeners widely used as industrial chemicals. PCBs are found as by-products in dye and paint manufacture and are legacy, ubiquitous, and persistent as human and environmental contaminants. PCBs with fewer chlorine atoms may be metabolized to hydroxy- and dihydroxy-metabolites and further oxidized to quinoid metabolites both in vitro and in vivo. Specifically, quinoid metabolites may form adducts on nucleophilic sites within cells. We hypothesized that the PCB-quinones covalently bind to cytochrome c and, thereby, cause defects in the function of cytochrome c. In this study, synthetic PCB quinones, 2-(4'-chlorophenyl)-1,4-benzoquinone (PCB3-pQ), 4-4'-chlorophenyl)-1,2-benzoquinone (PCB3-oQ), 2-(3', 5'-dichlorophenyl)-1,4-benzoquinone, 2-(3',4', 5'-trichlorophenyl)-1,4-benzoquinone, and 2-(4'-chlorophenyl)-3,6-dichloro-1,4-benzoquinone, were incubated with cytochrome c, and adducts were detected by liquid chromatography-mass spectrometry (LC-MS) and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI TOF). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was employed to separate the adducted proteins, while trypsin digestion and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied to identify the amino acid binding sites on cytochrome c. Conformation change of cytochrome c after binding with PCB3-pQ was investigated by SYBYL-X simulation and cytochrome c function was examined. We found that more than one molecule of PCB-quinone may bind to one molecule of cytochrome c. Lysine and glutamic acid were identified as the predominant binding sites. Software simulation showed conformation changes of adducted cytochrome c. Additionally, cross-linking of cytochrome c was observed on the SDS-PAGE gel. Cytochrome c was found to lose its function as electron acceptor after incubation with PCB quinones. These data provide evidence that the covalent binding of PCB quinone metabolites to cytochrome c may be included among the toxic effects of PCBs.

Indexed as

Chromatography, LiquidCytochromes cHumansMolecular StructureOxidation-ReductionPolychlorinated BiphenylsTandem Mass SpectrometryCytochromes cPolychlorinated Biphenyls4-ChlorobiphenylCytochrome cPost-translational modificationProtein adductsProtein cross-linkingQuinoid metabolites

Identifiers

PMID26062463
PMCPMC4676959
OpenAlexW590804838

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.