Electron transfer between horse ferritin and ferrihaemoproteins

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...

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Bibliographic Details
Published in:Biochemical Journal
Main Authors: Kadir, F H A, al-Massad, F K, Fatemi, S J A, Singh, H K, Wilson, M T, Moore, G R
Format: Article in Journal/Newspaper
Language:English
Published: Portland Press Ltd. 1991
Subjects:
Cell Biology
Molecular Biology
Biochemistry
Sperm whale
Online Access:http://dx.doi.org/10.1042/bj2780817
https://portlandpress.com/biochemj/article-pdf/278/3/817/603913/bj2780817.pdf
Description
Summary: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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