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Home / Equine Research Bank / Biochem J / Animal ferritin and bacterioferritin contain quinones.
The Biochemical journal1992; 283 ( Pt 1)(Pt 1); 177-180; doi: 10.1042/bj2830177

Animal ferritin and bacterioferritin contain quinones.

Abstract: The origin of the 440 nm fluorescence of horse spleen ferritin and of Pseudomonas aeruginosa and Azotobacter vinelandii bacterioferritin has been investigated using a Nitro Blue Tetrazolium/glycinate colorimetric test specific for quiones [Paz, Flückiger, Boak, Kagan & Gallop (1991) J. Biol. Chem. 266, 689-692]. The results of the analysis indicate that ferritin and bacterioferritins contain quinones. A possible functional role of these quinones in iron uptake and release is described, as is the possibility that the presence of quinones in these proteins results from oxidative damage.
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Publication Date: 1992-04-01 PubMed ID: 1567365PubMed Central: PMC1131011DOI: 10.1042/bj2830177Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research investigates the presence of quinones in animal (horse spleen) ferritin and bacterioferritin (from certain bacteria types), and also suggests their possible functional roles in the transition of iron.

Understanding the Research

  • This research delves into understanding the origin of the 440nm fluorescence, specifically in horse spleen ferritin and bacterioferritins observed in Pseudomonas aeruginosa and Azotobacter vinelandii bacteria.
  • The researchers used a Nitro Blue Tetrazolium/glycinate colorimetric test, which is a test specific for quinones. The objective of using this test was to identify or confirm the presence of quinones in these ferritins.
  • The results from the test confirmed the presence of quinones in both animal ferritins and bacterioferritins, hence confirming their hypothesis.

Possible Functional Roles of Quinones

  • Following the identification of quinones, the paper starts to theorize about their actual role in ferritins.
  • The possible function of quinones as per the study could be in connection with the iron uptake and release.
  • Iron uptake and release is a crucial aspect for numerous biological processes and understanding the function of quinones in this context could potentially provide novel insights for further biological and biochemical research.

Quinones Origin – A Result of Oxidative Damage?

  • Additionally, the study also discusses the potential source of these identified quinones. They suggest that the presence of quinones in these proteins might result from oxidative damage.
  • Oxidative damage is a process that happens as a result of the imbalance between the production of reactive oxygen species (free radicals) and antioxidant defenses.
  • This may lead to further studies aimed at understanding the implications of the oxidative damage on these ferritins, and how it affects their function, particularly in relation to the iron uptake and release.

Cite This Article

APA
al-Massad FK, Kadir FH, Moore GR. (1992). Animal ferritin and bacterioferritin contain quinones. Biochem J, 283 ( Pt 1)(Pt 1), 177-180. https://doi.org/10.1042/bj2830177

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 283 ( Pt 1)
Issue: Pt 1
Pages: 177-180

Researcher Affiliations

al-Massad, F K
  • Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, U.K.
Kadir, F H
    Moore, G R

      MeSH Terms

      • Animals
      • Azotobacter / chemistry
      • Bacterial Proteins / analysis
      • Bacterial Proteins / chemistry
      • Cytochrome b Group / analysis
      • Cytochrome b Group / chemistry
      • Ferritins / analysis
      • Ferritins / chemistry
      • Fluorometry
      • Horses
      • Pseudomonas aeruginosa / chemistry
      • Quinones / analysis
      • Quinones / chemistry
      • Spectrometry, Fluorescence
      • Spleen / chemistry

      Grant Funding

      • Wellcome Trust

      References

      This article includes 20 references
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      Citations

      This article has been cited 4 times.
      1. Kato Y, Suga N. Covalent adduction of endogenous and food-derived quinones to a protein: its biological significance. J Clin Biochem Nutr 2018 May;62(3):213-220.
        doi: 10.3164/jcbn.18-26pubmed: 29892159google scholar: lookup
      2. Bradley JM, Le Brun NE, Moore GR. Ferritins: furnishing proteins with iron. J Biol Inorg Chem 2016 Mar;21(1):13-28.
        doi: 10.1007/s00775-016-1336-0pubmed: 26825805google scholar: lookup
      3. Moore GR, Kadir FH, al-Massad FK, Le Brun NE, Thomson AJ, Greenwood C, Keen JN, Findlay JB. Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin. Biochem J 1994 Dec 1;304 ( Pt 2)(Pt 2):493-7.
        doi: 10.1042/bj3040493pubmed: 7998985google scholar: lookup
      4. Cheesman MR, Kadir FH, al-Basseet J, al-Massad F, Farrar J, Greenwood C, Thomson AJ, Moore GR. E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii. Biochem J 1992 Sep 1;286 ( Pt 2)(Pt 2):361-7.
        doi: 10.1042/bj2860361pubmed: 1326939google scholar: lookup
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