Evidence map›Paper›PMID 15205408›Full record

ArticleJournal of bacteriology2004

Free and hemophore-bound heme acquisitions through the outer membrane receptor HasR have different requirements for the TonB-ExbB-ExbD complex.

Sylvie Létoffé, Philippe Delepelaire, Cécile Wandersman

Abstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-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

26 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
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  6. Gallium-Protoporphyrin IX InhibitsFrontiers in cellular and infection microbiology · 2017
    Article
  7. Article
  8. Article
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  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Bacterial heme-transport proteins and their heme-coordination modes.Archives of biochemistry and biophysics · 2009
    Review
  19. Article
  20. 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 2 institutions in 1 country.

Sylvie LétofféUnité des Membranes Bactériennes, Institut Pasteur (CNRS URA2172), 75724 Paris 15, France.
Philippe Delepelaire
Cécile Wandersman
Institut Pasteur · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many gram-negative bacteria have specific outer membrane receptors for free heme, hemoproteins, and hemophores. Heme is a major iron source and is taken up intact, whereas hemoproteins and hemophores are not transported: the iron-containing molecule has to be stripped off at the cell surface, with only the heme moiety being taken up. The Serratia marcescens hemophore-specific outer membrane receptor HasR can transport either heme itself or heme bound to the hemophore HasA. This second mechanism is much more efficient and requires a higher TonB-ExbB-ExbD (TonB complex) concentration than does free or hemoglobin-bound heme uptake. This requirement for more of the TonB complex is associated with a higher energy requirement. Indeed, the sensitivity of heme-hemophore uptake to the protonophore carbonyl cyanide m-chlorophenyl hydrazone is higher than that of heme uptake from hemoglobin. We show that a higher TonB complex concentration is required for hemophore dissociation from the receptor. This dissociation is concomitant with heme uptake. We propose that increasing the TonB complex concentration drives more energy to the outer membrane receptor and speeds up the release of empty hemophores, which, if they remained on receptors, would inhibit heme transport.

Indexed as

Bacterial ProteinsEscherichia coli ProteinsHemeMembrane ProteinsReceptors, Cell SurfaceBacterial ProteinsEscherichia coli ProteinsExbB protein, E coliexbD protein, E coliHemeheme receptorMembrane ProteinsReceptors, Cell SurfacetonB protein, BacteriatonB protein, E coli

Identifiers

PMID15205408
PMCPMC421607
OpenAlexW2113069833

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.