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The Biochemical journal1991; 278 ( Pt 3)(Pt 3); 817-820; doi: 10.1042/bj2780817

Electron transfer between horse ferritin and ferrihaemoproteins.

Abstract: Reactions of reduced horse spleen ferritin with horse and Saccharomyces cerevisiae ferricytochromes c, cow ferricytochrome b5, sperm-whale metmyoglobin and Pseudomonas aeruginosa ferricytochrome c-551 were investigated by u.v.-visible spectrophotometry. In all cases the reduced ferritin reduced the ferrihaemoproteins. The rate of reduction varied from less than 0.2 M-1.s-1 for metmyoglobin to 1.1 x 10(3) M-1.s-1 for horse ferricytochrome c (0.1 M-phosphate buffer, pH 7.4, at 25 degrees C). We conclude that the mechanism of ferrihaemoprotein reduction involves long-range electron transfer through the coat of ferritin and that such electron transfer is rapid enough to account for the rates of iron release observed by other workers in reductive release assays.
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Publication Date: 1991-09-15 PubMed ID: 1654893PubMed Central: PMC1151419DOI: 10.1042/bj2780817Google 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.

The research paper studies how the electron transfer occurs between horse ferritin—a protein that stores iron—and different types of ferrihaemoproteins, which are iron-containing hemoproteins. The study uses spectrophotometry—which measures how much light a chemical substance absorbs—to determine that the mechanism of reduction involves a long-range electron transfer through the ferritin and is fast enough to match the rates of iron release observed in previous studies.

Investigation of Electron Transfer

  • The researchers observed the reactions of reduced horse spleen ferritin with different types of ferricytochromes or ferrihaemoproteins, from various organisms such as horses, Saccharomyces cerevisiae (a species of yeast), cows, sperm-whale, and Pseudomonas aeruginosa (a bacterium).
  • They used ultra-violet-visible spectrophotometry, a method that allows researchers to measure the amount of light that a chemical substance absorbs. This helped the researchers to monitor and understand the electron transfer reactions happening between the ferritin and the ferrihaemoproteins.

Results and Conclusions

  • It was observed that in all cases the reduced ferritin reduced the ferrihaemoproteins, indicating successful electron transfer.
  • However, the rate of reduction varied from one ferrihaemoprotein to another. For instance, less than 0.2 M-1.s-1 was recorded for metmyoglobin from the sperm-whale, whereas 1.1 x 10(3) M-1.s-1 was recorded for horse ferricytochrome c.
  • From these observations, researchers concluded that the mechanism of ferrihaemoprotein reduction involves a process of long-range electron transfer through the protein coat of the ferritin.
  • They also concluded that this electron transfer process is fast enough to match the rates of iron release that other researchers have observed in their studies involving reductive release assays.

Significance of the Study

  • Understanding the mechanism of electron transfer between ferritin and ferrihaemoproteins could provide valuable insights into how iron is stored and released in organisms, which is vital for many biological processes.

Cite This Article

APA
Kadir FH, al-Massad FK, Fatemi SJ, Singh HK, Wilson MT, Moore GR. (1991). Electron transfer between horse ferritin and ferrihaemoproteins. Biochem J, 278 ( Pt 3)(Pt 3), 817-820. https://doi.org/10.1042/bj2780817

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 278 ( Pt 3)
Issue: Pt 3
Pages: 817-820

Researcher Affiliations

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

            MeSH Terms

            • Animals
            • Bacterial Proteins
            • Cytochrome c Group / metabolism
            • Cytochromes / metabolism
            • Cytochromes b5 / metabolism
            • Electron Transport
            • Ferritins / metabolism
            • Horses
            • Myoglobin / metabolism
            • Oxidation-Reduction
            • Spectrophotometry, Ultraviolet

            Grant Funding

            • Wellcome Trust

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            Citations

            This article has been cited 1 times.
            1. Huang HQ, Lin QM, Lou ZB. Construction of a ferritin reactor: an efficient means for trapping various heavy metal ions in flowing seawater. J Protein Chem 2000 Aug;19(6):441-7.
              doi: 10.1023/a:1026541129563pubmed: 11195968google scholar: lookup
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