Chemical and Biochemical Properties of the Iron Mineral Core of Mammalian Ferritin

Abstract

The Research objectives are to evaluate the chemical composition of the iron core of mammalian ferritin with regard to: 1 < binding of metal ions; 2) electrochemical energy storage and 3) electron transfer reactions. Both apo and holo ferritin bind Fe+ as well as other metal ions (Cu2+, Zn2+and Mn2+) under anaerobic conditions as a function of pH. Apo ferritin binds 8Fe2+ at protein sites whereas holo binds large numbers of Fe2+ on its mineral core surface. Holo ferritin undergoes reduction at its FeOOH mineral core forming a Fe2+ mineral phase. Apo ferritin also undergoes redox reactions presumable at some amino acid cite. Electron transfer reaction occur readily in the FeOOH core indicating the mineral core has relatively high electrical conductivity. Keywords: Ferritin; Electron Transfer; Redox Reactions; Biomineral.

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Document Details

Document Type
Technical Report
Publication Date
Jun 05, 1989
Accession Number
ADA211065

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  • Gerald D. Watt

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  • University of Colorado Boulder

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