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三个铁结合位点的存在如何影响大肠杆菌铁蛋白(EcFtnA)的铁储存功能。

How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli.

作者信息

Treffry A, Zhao Z, Quail M A, Guest J R, Harrison P M

机构信息

The Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.

出版信息

FEBS Lett. 1998 Aug 7;432(3):213-8. doi: 10.1016/s0014-5793(98)00867-9.

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.

摘要

铁储存蛋白——铁蛋白,存在于所有利用铁的生物体中。本文将大肠杆菌铁蛋白(EcFtnA)中的铁储存过程与人类H型铁蛋白(HuHF)中的过程进行了比较。两种蛋白都含有双核铁中心,能使O₂将2个Fe(II)快速氧化。EcFtnA中第三个铁结合位点的存在,虽对快速氧化并非必不可少,但会使O₂/Fe比率从2增至3 - 4。在EcFtnA中,每个分子氧化48个Fe(II)原子后,铁氧化速率显著下降,这可能是因为部分铁仍留在氧化位点。然而,这带来了一种补偿性的生理优势,因为这种铁更易于满足细胞的需求。

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