Calvo Jenifer, Jung Hunmin, Meloni Gabriele
Department of Chemistry and Biochemistry, University of Texas at Dallas, Richardson, TX, USA.
IUBMB Life. 2017 Apr;69(4):236-245. doi: 10.1002/iub.1618. Epub 2017 Mar 13.
Metallothioneins (MTs) are a class of low molecular weight and cysteine-rich metal binding proteins present in all the branches of the tree of life. MTs efficiently bind with high affinity several essential and toxic divalent and monovalent transition metals by forming characteristic polynuclear metal-thiolate clusters within their structure. MTs fulfil multiple biological functions related to their metal binding properties, with essential roles in both Zn(II) and Cu(I) homeostasis as well as metal detoxification. Depending on the organism considered, the primary sequence, and the specific physiological and metabolic status, Cu(I)-bound MT isoforms have been isolated, and their chemistry and biology characterized. Besides the recognized role in the biochemistry of divalent metals, it is becoming evident that unique biological functions in selectively controlling copper levels, its reactivity as well as copper-mediated biochemical processes have evolved in some members of the MT superfamily. Selected examples are reviewed to highlight the peculiar chemical properties and biological functions of copper MTs. © 2016 IUBMB Life, 69(4):236-245, 2017.
金属硫蛋白（MTs）是一类低分子量且富含半胱氨酸的金属结合蛋白，存在于生命之树的所有分支中。MTs通过在其结构内形成特征性的多核金属硫醇盐簇，以高亲和力有效地结合多种必需和有毒的二价及一价过渡金属。MTs履行与其金属结合特性相关的多种生物学功能，在锌（II）和铜（I）的体内平衡以及金属解毒中均发挥重要作用。根据所考虑的生物体、一级序列以及特定的生理和代谢状态，已分离出结合铜（I）的MT同工型，并对其化学性质和生物学特性进行了表征。除了在二价金属生物化学中公认的作用外，越来越明显的是，MT超家族的一些成员已经进化出在选择性控制铜水平、其反应性以及铜介导的生化过程方面的独特生物学功能。本文综述了一些选定的例子，以突出铜MTs的特殊化学性质和生物学功能。© 2016国际生物化学与分子生物学联盟生命科学部，69(4):236 - 245，2017。
