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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Portland Press Ltd.
1991
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Online Access: | http://dx.doi.org/10.1042/bj2780817 https://portlandpress.com/biochemj/article-pdf/278/3/817/603913/bj2780817.pdf |
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crportlandpress:10.1042/bj2780817 2023-12-31T10:23:22+01:00 Electron transfer between horse ferritin and ferrihaemoproteins Kadir, F H A al-Massad, F K Fatemi, S J A Singh, H K Wilson, M T Moore, G R 1991 http://dx.doi.org/10.1042/bj2780817 https://portlandpress.com/biochemj/article-pdf/278/3/817/603913/bj2780817.pdf en eng Portland Press Ltd. Biochemical Journal volume 278, issue 3, page 817-820 ISSN 0264-6021 1470-8728 Cell Biology Molecular Biology Biochemistry journal-article 1991 crportlandpress https://doi.org/10.1042/bj2780817 2023-12-04T13:29:28Z 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. Article in Journal/Newspaper Sperm whale Portland Press (via Crossref) Biochemical Journal 278 3 817 820 |
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Open Polar |
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Portland Press (via Crossref) |
op_collection_id |
crportlandpress |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry Kadir, F H A al-Massad, F K Fatemi, S J A Singh, H K Wilson, M T Moore, G R Electron transfer between horse ferritin and ferrihaemoproteins |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Kadir, F H A al-Massad, F K Fatemi, S J A Singh, H K Wilson, M T Moore, G R |
author_facet |
Kadir, F H A al-Massad, F K Fatemi, S J A Singh, H K Wilson, M T Moore, G R |
author_sort |
Kadir, F H A |
title |
Electron transfer between horse ferritin and ferrihaemoproteins |
title_short |
Electron transfer between horse ferritin and ferrihaemoproteins |
title_full |
Electron transfer between horse ferritin and ferrihaemoproteins |
title_fullStr |
Electron transfer between horse ferritin and ferrihaemoproteins |
title_full_unstemmed |
Electron transfer between horse ferritin and ferrihaemoproteins |
title_sort |
electron transfer between horse ferritin and ferrihaemoproteins |
publisher |
Portland Press Ltd. |
publishDate |
1991 |
url |
http://dx.doi.org/10.1042/bj2780817 https://portlandpress.com/biochemj/article-pdf/278/3/817/603913/bj2780817.pdf |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biochemical Journal volume 278, issue 3, page 817-820 ISSN 0264-6021 1470-8728 |
op_doi |
https://doi.org/10.1042/bj2780817 |
container_title |
Biochemical Journal |
container_volume |
278 |
container_issue |
3 |
container_start_page |
817 |
op_container_end_page |
820 |
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1786834938987806720 |