Iron complexes hydrolytic polymerization

Variations in ferritin protein coats coincide with variations in iron metabolism and gene expression, suggesting an Interdependence. Iron core formation from protein coats requires Fe(Il), at least experimentally, which follows a complex path of oxidation and hydrolytic polymerization the roles of the protein and the electron acceptor are only partly understood. It is known that mononuclear and small polynuclear Fe clusters bind to the protein early in core formation. However, variability in the stoichiometry of Fe/oxidant and the apparent sequestration and stabilization of Fe(II) in the protein for long periods of time indicate a complex microenvironment maintained by the protein coats. Full understanding of the relation of the protein to core formation, particularly at intermediate stages, requires a systematic analysis using defined or engineered protein coats. 

Hydrol5dic polymerization in the ferric citrate system can be prevented if sufficient excess citrate is present in solution 66). Approximately 20 millimolar excess citrate is sufficient to supress pol3mier-ization of 1 millimolar iron, as indicated by dialysis and spectrophotomet-ric measurements. From pH titration in high citrate solutions, it was concluded 66) that a dicitrate complex of iron is formed at high pH. Presumably formation of the dicitrate chelate is competitive with hydrolytic polymerization. The fraction of polymer formed in ferric citrate solutions was found to decrease smoothly as the citrate content was increased up to 20 millimolar. The nuclear relaxation rate of the water protons in ferric citrate solutions increases with the citrate concentration. 

The defined architecture of the metalloprotein ferritin, a natural complex of iron oxide, is found in almost all domains of life and has been used as a constrained reaction vessel for the synthesis of a number of non-natural metal oxides [28, 34]. The protein ferritin consists of 24 subunits that self-assemble into a cage, consisting of a threefold hydrophilic channel coordinated to a fourfold hydrophobic channel [20, 28]. In biology, Fe(ll) is introduced into the core of the apoprotein through its hydrophiUc charmels where the ferrous ion is catalytically oxidized to a less-soluble ferric ion, Fe(lll) [20]. The ferric ion then undergoes a series of hydrolytic polymerizations to form the insoluble ferric oxyhydroxide mineral (ferrihydrite), which is physically constrained by the size of the protein cage (12 nm outer diameter, 8nm inner diameter) [35]. The enzyme ferrous oxidase is coordinated within the protein cage, the interior and exterior of which is electrostatically dissimilar, to produce spatially defined minerals. 

A review of iron(III) in aqueous solution covers hydrolysis and polymerization, the formation and dissociation of binuclear species, and kinetics and mechanisms of water exchange and complex formation. " Kinetic and equilibrium data for hydrolytic reactions of iron(III) have been conveniently assembled. Reviews of hydrolysis of Fe aq, and subsequent precipitation of hydrated oxide-hydroxide species, cover a very wide range of media, from geochemistry to biology to human metabolism. Added anions or pH variation can affect which form... 

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