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How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli
Author(s) -
Treffry Amyra,
Zhao Zhongwei,
Quail Michael A,
Guest John R,
Harrison Pauline M
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00867-9
Subject(s) - ferritin , escherichia coli , chemistry , biochemistry , iron binding proteins , function (biology) , biology , microbiology and biotechnology , transferrin , gene
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 O 2 . The presence of a third iron binding site in EcFtnA, although not essential for fast oxidation, causes the O 2 /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.