Evidence map›Paper›PMID 17387526›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2007

Cloning and characterization of a novel periplasmic heme-transport protein from the human pathogen Pseudomonas aeruginosa.

Yong Tong, Maolin Guo

Abstract read
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Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Impact of NaJournal of bacteriology · 2020
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Role and regulation of heme iron acquisition in gram-negative pathogens.Frontiers in cellular and infection microbiology · 2013
    Review
  10. Article
  11. Article
  12. Recent advances in bacterial heme protein biochemistry.Current opinion in chemical biology · 2011
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Bacterial heme-transport proteins and their heme-coordination modes.Archives of biochemistry and biophysics · 2009
    Review
  18. 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

2 authors at 2 institutions in 1 country.

Yong TongDepartment of Chemistry and Biochemistry, University of Massachusetts, Dartmouth, MA 02747-2300, USA.
Maolin Guo
University of Massachusetts Amherst · USUniversity of Massachusetts Dartmouth · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Successful iron acquisition plays a crucial role in bacterial virulence. Numerous Gram-negative pathogenic bacteria have developed a novel heme-acquisition system to steal iron from hosts. This system involves a cell-surface heme receptor, a periplasmic heme-transport protein (HTP) and inner-membrane proteins typical for ATP binding cassette transporters. We have cloned the gene encoding a periplasmic HTP from Pseudomonas aeruginosa, overexpressed it in Escherichia coli and purified it as a 33-kDa His-tagged protein. Heme-staining and heme-content assays reveal that the isolated HTP contains approximately 50% heme-bound and apo forms. The heme is noncovalently attached and can be transferred to apomyoglobin in vitro. Electron paramagnetic resonance and UV-vis spectroscopies indicate a five-coordinate, high-spin, ferric heme in HTP. HTP is reduced by dithionite but not by either dithiothreitol or ascorbate. Fluorescence and circular dichroism spectroscopies indicate a well-ordered structure for the HTP and a conformational change upon heme binding to apo-HTP. This was confirmed by limited proteolysis assays. Apo-HTP binds heme or protoporphyrin IX at 1:1 ratio with high affinity (K (d) approximately 1.2 and 14 nM, respectively). A BLASTP search revealed approximately 52 putative bacterial periplasmic heme transporters, which can be grouped into six classes, most of which are associated with pathogenic bacteria. Multiple sequence alignment reveals that these HTPs share low sequence similarity and no conserved common binding motif for heme ligation. However, a tyrosine residue (Y71) is highly conserved in the HTP sequences, which is likely an axial heme ligand in HTPs. Mutagenesis studies support Y71-heme iron ligation in the recombinant HTP.

Indexed as

Bacterial ProteinsCarrier ProteinsCloning, MolecularHemeHumansPeriplasmic ProteinsProtoporphyrinsPseudomonas aeruginosaSequence AlignmentSpectrum AnalysisBacterial ProteinsCarrier ProteinsHemePeriplasmic Proteinsprotoporphyrin IXProtoporphyrins

Identifiers

PMID17387526
OpenAlexW2017839314

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.