Haem binding to horse spleen ferritin
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(90)80512-H/fullpdf
Reference19 articles.
1. Ferritin: design and formation of an iron-storage molecule
2. Azotobacter cytochrome b557.5 is a bacterioferritin
3. Undifferentiated F9 embryonal carcinoma cells produce a short-chain collagen molecule
4. Isolation and properties of the complex nonheme-iron-containing cytochrome b557 (bacterioferritin) from pseudomonas aeruginosa
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2. Precise engineering of apoferritin through site-specific host–guest binding;Chemical Communications;2020
3. Heme-coordinated histidine residues form non-specific functional ⿿ferritin-heme⿿ peroxidase system: Possible and partial mechanistic relevance to oxidative stress-mediated pathology in neurodegenerative diseases;International Journal of Biological Macromolecules;2016-10
4. Direct evidence for non-specific peroxidase activity of ‘‘ferritin–heme” complex: possible role in the development of neurodegenerative diseases;Journal of the Iranian Chemical Society;2014-09-28
5. On the repair of oxidative damage to apoferritin: a model study with the flavonoids quercetin and rutin in aerated and deaerated solutions;Free Radical Research;2013-05-02
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