Evidence map›Paper›PMID 27791000›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Radical new paradigm for heme degradation in Escherichia coli O157:H7.

Joseph W LaMattina, David B Nix, William Nicholas Lanzilotta

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Biochemical and functional characterization ofFrontiers in microbiology · 2026
    Article
  4. Review
  5. Article
  6. Article
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  8. Article
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  10. Article
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  12. Article
  13. Article
  14. Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Functional Diversity of HemN-like Proteins.ACS bio & med chem Au · 2022
    Review
  20. 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

3 authors at 1 institution in 1 country.

Joseph W LaMattinaDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602; Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602.
David B NixDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602; Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
William Nicholas LanzilottaDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602; Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602; wlanzilo@bmb.uga.edu.
University of Georgia · US

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
NIGMS NIH HHS P41 GM103490
6 · The paper itself

Abstract

All of the heme-degrading enzymes that have been characterized to date require molecular oxygen as a cosubstrate. Escherichia coli O157:H7 has been shown to express heme uptake and transport proteins, as well as use heme as an iron source. This enteric pathogen colonizes the anaerobic space of the lower intestine in mammals, yet no mechanism for anaerobic heme degradation has been reported. Herein we provide evidence for an oxygen-independent heme-degradation pathway. Specifically, we demonstrate that ChuW is a radical S-adenosylmethionine methyltransferase that catalyzes a radical-mediated mechanism facilitating iron liberation and the production of the tetrapyrrole product we termed "anaerobilin." We further demonstrate that anaerobilin can be used as a substrate by ChuY, an enzyme that is coexpressed with ChuW in vivo along with the heme uptake machinery. Our findings are discussed in terms of the competitive advantage this system provides for enteric bacteria, particularly those that inhabit an anaerobic niche in the intestines.

Indexed as

Gene Expression Regulation, BacterialAnaerobiosisBiological TransportEscherichia coli O157Escherichia coli ProteinsFlavodoxinFree RadicalsHemeHemeproteinsIronOxidoreductases Acting on CH-CH Group DonorsProtein O-MethyltransferaseTetrapyrrolesanaerobilinChuX protein, E coliChuY protein, E coliEscherichia coli ProteinsFlavodoxinFree RadicalsHemeHemeproteinsIronOxidoreductases Acting on CH-CH Group DonorsProtein O-MethyltransferaseTetrapyrrolesanaerobichemeintestinal microbiomepathogenradical SAM

Identifiers

PMID27791000
PMCPMC5087033
OpenAlexW2530969703

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.