Evidence map›Paper›PMID 9560292›Full record

ArticleThe Biochemical journal1998

The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the mu-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism.

J W Smalley, J Silver, P J Marsh, A J Birss

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.5field-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

63 citing papers in PubMed, 125 citations in OpenAlex.

  1. Trial
  2. Article
  3. The survival status ofJournal of oral microbiology · 2026
    Review
  4. Review
  5. Protoporphyrin IX iron(II) revisited. An overview of the Mössbauer spectroscopic parameters of low-spin porphyrin iron(II) complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Review
  6. Journal of pharmacy & bioallied sciences · 2024
    Review
  7. Review
  8. Frontiers in cellular and infection microbiology · 2024
    Article
  9. Photoinactivation and Photoablation ofPathogens (Basel, Switzerland) · 2023
    Review
  10. Studies on the binding of CO to low-spin [Fe(II)(Por)LJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Studies on the binding of nitrogenous bases to protoporphyrin IX iron(II) in aqueous solution at high pH values.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  16. Probiotics During the Therapeutic Management of Periodontitis.Advances in experimental medicine and biology · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Efficacy of an LED toothbrush on aJournal of periodontal & implant science · 2018
    Article

3 more citing papers are in PubMed but not listed here.

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.

J W SmalleyUnit of Oral Biology, Department of Clinical Dental Sciences, The University of Liverpool, Liverpool L69 3BX, UK.
J Silver
P J Marsh
A J Birss
University of Greenwich · GBUniversity of Liverpool · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mössbauer spectroscopy was used to re-evaluate iron protoporphyrin IX, FePPIX, binding and the chemical nature of the black iron porphyrin pigment of Porphyromonas gingivalis. We demonstrate that FePPIX is bound to the cell in the mu-oxo dimeric form, [Fe(III)PPIX]2O, and that the iron porphyrin pigment is also composed of this material. P. gingivalis also assimilated monomeric Fe(II)- and Fe(III)PPIX into mu-oxo dimers in vitro. Scatchard analysis revealed a greater binding maximum of cells for mu-oxo dimers than for monomeric Fe(III)-or Fe(II)PPIX, although the relative affinity constant for the dimers was lower. Formation of [Fe(III)PPIX]2O via reactions of Fe(II)PPIX with oxygen, and its toxic derivatives, would serve as an oxidative buffer and permit P. gingivalis and other black-pigmenting anaerobes to engender and maintain a local anaerobic environment. Tying up of free oxygen species with iron protoporphyrin IX would also reduce and limit Fe(II)PPIX-mediated oxygen-radical cell damage. More importantly, formation of a cell-surface mu-oxo dimer layer may function as a protective barrier against assault by reactive oxidants generated by neutrophils. Selective interference with these mechanisms would offer the possibility of attenuating the pathogenicity of P. gingivalis and other iron protoporphyrin IX-binding pathogens whose virulence is regulated by this reactive molecule.

Indexed as

AnaerobiosisDimerizationIronOxidation-ReductionPeriodontal DiseasesPigments, BiologicalPorphyromonas gingivalisProtein BindingProtoporphyrinsReactive Oxygen SpeciesSpectrum AnalysisIronPigments, Biologicalprotoporphyrin IXProtoporphyrinsReactive Oxygen Species

Identifiers

PMID9560292
PMCPMC1219405
OpenAlexW2151693749

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.