Article: Study data from University of East Anglia update knowledge of Escherichia coli.

According to recent research published in the journal Biochemistry, "Ferritins solubilize and detoxify the essential metal iron through formation of a ferric mineral within the protein's central cavity, Key to this activity is an intrasubunit catalytic dinuclear iron center called the ferroxidase center. Here we show that the fluorescence intensity of Escherichia coli bacterioferritin (BFR), due to the presence of two tryptophan residues (Trp35 and Trp133) in each of the 24 subunits, is highly sensitive to the iron status of the ferroxidase center and is quenched to different extents by Fe2+ and Fe3+."

"Recovery of the quench following oxidation of Fe2+ to Fe3+ at ...

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