Abstract
The toxic effects of the essential metal, iron, are controlled within cells through its being bound by proteins or organic chelators [Halliwell and Gutteridge, 1986]. Within mammals, most intracellular iron not utilized for heme-containing enzymes is bound by the iron-storage protein, ferritin [Harrison et al., 1987; Theil, 1987; Joshi and Zimmerman, 1988]. Up to several thousand atoms of ferric iron can be contained within each ferritin molecule as one or more crystallites of the biomineral, ferrihydrite (5Fe2O3·9H2O) [Towe, 1981; Ford et al., 1984]. Unlike commonplace rust, the “biological iron oxide” within ferritin remains soluble. This very special and important capability is a direct consequence of the quaternary structure of the metalloprotein; in each ferritin molecule, the insoluble ferrihydrite forms a core that is contained inside an outer assembly of 24 polypeptide subunits (Mr≈ 20kDa) [Ford et al., 1984]. The core crystallites within the central cavity are attached to the surrounding protein shell [Stuhrmann et al., 1976; Massover, 1978].
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Massover, W.H. (1991). Dynamic Stability of Apoferritin: A New Model to Explain How Impermeable Reagents Can Reduce/Capture Iron within Ferritin. In: Frankel, R.B., Blakemore, R.P. (eds) Iron Biominerals. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3810-3_25
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DOI: https://doi.org/10.1007/978-1-4615-3810-3_25
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