Bradley Justin M, Moore Geoffrey R, Le Brun Nick E
Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.
Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.
Curr Opin Chem Biol. 2017 Apr;37:122-128. doi: 10.1016/j.cbpa.2017.02.027. Epub 2017 Mar 15.
The essential metal iron presents two major problems for life: it is potentially highly toxic due to its redox activity, and its extremely low solubility in aqueous solution in the presence of O can make it hard to acquire and store safely. Ferritins are part of nature's answer to these problems, as they store iron in a safe but accessible form in all types of cells. How they achieve this has been the subject of intense research for several decades. Here, we highlight recent progress in elucidating the routes by which Fe ions access the catalytic ferroxidase centers, and the mechanisms by which Fe is oxidized. Emerging from this is a picture of diversity, both in terms of Fe entry pathways and the roles played by the structurally distinct diiron ferroxidase centers.
由于其氧化还原活性，它具有潜在的高毒性，并且在有氧存在的情况下，其在水溶液中的极低溶解度会使其难以安全获取和储存。铁蛋白是自然界解决这些问题的一部分，因为它们在所有类型的细胞中以安全但可获取的形式储存铁。几十年来，它们如何做到这一点一直是深入研究的主题。在这里，我们强调了在阐明铁离子进入催化亚铁氧化酶中心的途径以及铁被氧化的机制方面的最新进展。由此呈现出一幅在铁进入途径以及结构不同的双铁亚铁氧化酶中心所起作用方面都具有多样性的图景。
