Abstract
Ferritin-Fe(III) was rapidly and quantitatively reduced and liberated as Fe(II) by FMNH2, FADH2 and reduced riboflavin. Dithionite also released Fe(II) from ferritin but at less than 1% of the rate with FMNH2. Cysteine, glutathione and ascorbate gave a similar slower rate and yielded less than 20% of the total iron from ferritin within a few hours. The reduction of ferritin-Fe(III) by the three riboflavin compounds gave complex second-order kinetics with overlapping fast and slow reactions. The fast reaction appeared to be non-specific and may be due to a reduction of Fe(III) of a lower degree of polymerization, equilibrated with ferritin iron. The amount of this Fe3+ ion initially reduced was small, less than 0.3% of the total iron. Addition of FMN to the ferritin–dithionite system enhanced the reduction; this is due to the reduction of FMN by dithionite to form FMNH2 which then reduces ferritin-Fe(III). A comparison of the thermodynamic parameters of FMNH2–ferritin and dithionite–ferritin complex formation showed that FMNH2 required a lower activation energy and a negative entropy change, whereas dithionite required 50% more activation energy and showed a positive entropy change in ferritin reduction. The effectiveness of FMNH2 in ferritin–Fe(III) reduction may be due to a specific binding of the riboflavin moiety to the protein portion of the ferritin molecule.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Duggan D. E., Streeter K. B. Inhibition of ferritin reduction by pyrazolo(3,4d)pyrimidines. Arch Biochem Biophys. 1973 May;156(1):66–70. doi: 10.1016/0003-9861(73)90341-x. [DOI] [PubMed] [Google Scholar]
- GREEN S., MAZUR A. Relation of uric acid metabolism to release of iron from hepatic ferritin. J Biol Chem. 1957 Aug;227(2):652–668. [PubMed] [Google Scholar]
- Grace N. D., Greenwald M. A., Greenberg M. S. Effect of allopurinol on iron mobilization. Gastroenterology. 1970 Jul;59(1):103–108. [PubMed] [Google Scholar]
- Hoy T. G., Harrison P. M., Shabbir M., Macara I. G. The release of iron from horse spleen ferritin to 1,10-phenanthroline. Biochem J. 1974 Jan;137(1):67–70. doi: 10.1042/bj1370067. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jones M. M., Johnston D. O. Rate of release of iron from ferritin to 1, 10-phenanthroline. Nature. 1967 Nov 4;216(5114):509–510. doi: 10.1038/216509a0. [DOI] [PubMed] [Google Scholar]
- MAZUR A., BAEZ S., SHORR E. The mechanism of iron release from ferritin as related to its biological properties. J Biol Chem. 1955 Mar;213(1):147–160. [PubMed] [Google Scholar]
- MAZUR A., CARLETON A. HEPATIC XANTHINE OXIDASE AND FERRITIN IRON IN THE DEVELOPING RAT. Blood. 1965 Sep;26:317–322. [PubMed] [Google Scholar]
- MAZUR A., GREEN S., SAHA A., CARLETON A. Mechanism of release of ferritin iron in vivo by xanthine oxidase. J Clin Invest. 1958 Dec;37(12):1809–1817. doi: 10.1172/JCI103774. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Niederer W. Ferritin: iron incorporation and iron release. Experientia. 1970;26(2):218–220. doi: 10.1007/BF01895596. [DOI] [PubMed] [Google Scholar]
- Osaki S., Johnson D. A., Frieden E. The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase I. J Biol Chem. 1971 May 10;246(9):3018–3023. [PubMed] [Google Scholar]