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Iron binding to human heavy-chain ferritin

机译:人类重链铁蛋白铁绑定

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摘要

Maxi-ferr itins are ubiquitous iron-storage proteins with a common cage architecture made up of 24 identical subunits of five-helices that drive iron biomineralization through catalytic iron(II) oxidation occurring at oxido-reductase sites (OS). Structures of iron-bound human H ferritin were solved at high resolution by freezing ferritin crystals at different time intervals after exposure to a ferrous salt. Multiple binding sites were identi fied that define the iron path from the entry ion channels to the oxidoreductase sites. Similar data are available for another vertebrate ferritin: the M protein from Rana catesbeiana. A comparative analysis of the iron sites in the two proteins identifie s new reaction intermediates and underline s clear differences in the pattern of ligands that define the additional iron sites that precede the oxidoreductase binding sites along this path. Stopped-flow kinetics assays revealed that human H ferritin has different levels of activity compared with its R. catesbeiana counterpart. The role of the different pattern of transient iron-binding sites in the OS is discussed with respect to the observed differences in activity across the species.
机译:编号”Maxi-ferr随处可见铁储存蛋白质与一个共同的笼结构组成five-helices 24相同的子单元驱动器通过催化铁生物矿化铁(II)在oxido-reductase氧化发生网站(OS)。铁蛋白是解决高分辨率冰冷的铁蛋白晶体在不同的时间时间间隔在暴露于亚铁盐。多个结合位点是一致格同一标准的定义从离子通道入口的铁路径氧化还原酶的网站。可用于另一个脊椎动物铁蛋白:M从Rana catesbeiana蛋白质。两种蛋白质分析铁网站标识符新反应中间体和年代强调清晰的模式的差异配体定义额外的铁网站之前的氧化还原酶结合位点沿着这条路。表明人类H铁蛋白有不同水平的活动相比,其R。catesbeiana。不同模式的瞬态铁扎网站在操作系统的讨论观察活动的差异物种。

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