Metallothioneins with unusual residues: Histidines as modulators of zinc affinity and reactivity
Metallothioneins with unusual residues: Histidines as modulators of zinc affinity and reactivity
复制标题
DOI：
10.1016/j.jinorgbio.2007.10.032
复制
发表时间：
2008-03-01
影响因子：
3.9
通讯作者：
Blindauer, Claudia A.
中科院分区：
文献类型：
--
作者：
Blindauer, Claudia A.
多年来，关于金属硫蛋白的范例包括通过来自半胱氨酸残基的硫醇盐的排他性金属配位和不存在芳族残基。随着更多的序列和体外数据的金属硫蛋白，特别是从非脊椎动物的生物体，已成为可用的，金属硫蛋白中的组氨酸残基的发生和金属配位正在成为一个更频繁的功能比预期的。我们讨论了组氨酸与半胱氨酸在锌结合位点的一般意义，并回顾了一些最近的结果，从文献和我们自己的实验室。我们的结论是，组氨酸可以稳定金属硫蛋白簇，通过减少总电荷，提供的能力，以帮助结构组织提供H-键供体和受体的属性，减少二硫键形成的可能性，同时保持对金属离子的高亲和力，特别是边缘锌离子。(C)2007爱思唯尔公司All rights reserved.
For many years, paradigms regarding metallothioneins comprised the exclusive metal coordination by thiolates from cysteine residues and the absence of aromatic residues. As more sequence and in vitro data on metallothioneins, in particular from non-vertebrate organisms, has become available, both the occurrence of and metal coordination by histidine residues in metallothioneins is emerging as a more frequent feature than expected. We discuss the general implications of histidines versus cysteines in zinc binding sites, and review some recent results from literature and our own lab. We conclude that histidines can stabilise metallothionein clusters by reducing the overall charge, offering the ability to help with structural organisation by supplying H-bond donor and acceptor properties, reducing the likelihood for disulfide bond formation, whilst maintaining a high affinity towards metal ions, in particular the borderline zinc ion. (C) 2007 Elsevier Inc. All rights reserved.