PMID:9720927
| Citation |
Treffry, A, Zhao, Z, Quail, MA, Guest, JR and Harrison, PM (1998) How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli. FEBS Lett. 432:213-8 |
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| Abstract |
The iron storage proteins, ferritins, are found in all organisms which use iron. Here iron storage processes in the Escherichia coli ferritin (EcFtnA) are compared with those in human H-type ferritin (HuHF). Both proteins contain dinuclear iron centres that enable the rapid oxidation of 2 Fe(II) by O2. The presence of a third iron binding site in EcFtnA, although not essential for fast oxidation, causes the O2/Fe ratio to increase from 2 to 3-4. In EcFtnA the rate of iron oxidation falls markedly after the oxidation of 48 Fe(II) atoms/molecule probably because some of it remains at the oxidation site. However a compensatory physiological advantage is conferred because this iron is more readily available to meet the cell's needs. |
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| Keywords |
Amino Acid Sequence; Binding Sites; Escherichia coli/chemistry; Escherichia coli/metabolism; Ferritins/chemistry; Ferritins/metabolism; Ferrous Compounds/chemistry; Ferrous Compounds/metabolism; Iron/metabolism; Oxidation-Reduction; Oxygen/chemistry; Oxygen/metabolism; Protein Structure, Tertiary; Sequence Homology, Amino Acid |
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