Protein metalation in a nutshell.

Protein metalation in a nutshell.
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DOI:
10.1002/1873-3468.14500
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发表时间:
2023-01
期刊:
影响因子:
3.5
通讯作者:
Robinson, Nigel J.
Robinson, Nigel J.
中科院分区:
生物学3区
文献类型:
--
作者:
Osman, Deenah;Robinson, Nigel J.

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金属化,即蛋白质对金属的获取,必须避免与更紧密结合的金属发生错金属化。这是由四个选定的蛋白质,需要不同的金属说明:所有显示相似的排名顺序的亲和性的生物可利用的金属,在一个通用的亲和力系列(欧文-威廉姆斯系列)中所描述的。重要的是,细胞蛋白质金属化与其他金属结合位点竞争。这种竞争的强度定义了每种金属的细胞内可用性:其大小已通过校准细胞的DNA结合,金属传感,转录调节因子来估计。这已经确立了金属的可用性(作为形成金属络合物的自由能)保持在通用系列的倒数。最紧密结合的金属是最难获得的。有了这些可用性,就可以实现正确的金属化。在确定的细胞内金属利用率内,蛋白质的金属化是合乎逻辑的。避免了金属错配,因为较弱的结合金属比较紧的结合金属更容易获得。
Metalation, the acquisition of metals by proteins, must avoid mis‐metalation with tighter binding metals. This is illustrated by four selected proteins that require different metals: all show similar ranked orders of affinity for bioavailable metals, as described in a universal affinity series (the Irving–Williams series). Crucially, cellular protein metalation occurs in competition with other metal binding sites. The strength of this competition defines the intracellular availability of each metal: its magnitude has been estimated by calibrating a cells' set of DNA‐binding, metal‐sensing, transcriptional regulators. This has established that metal availabilities (as free energies for forming metal complexes) are maintained to the inverse of the universal series. The tightest binding metals are least available. With these availabilities, correct metalation is achieved. Metalation of proteins is logical within defined intracellular metal availabilities. Mis‐metalation is avoided because weaker binding metals are more available than tighter binding ones.
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