Copper transfer between Neurospora copper metallothionein and type 3 copper apoproteins
Copper transfer between Neurospora copper metallothionein and type 3 copper apoproteins
复制标题
脉孢菌铜金属硫蛋白和 3 型铜脱辅基蛋白之间的铜转移
DOI：
10.1016/0014-5793(82)80138-5
复制
发表时间：
1982
期刊：
影响因子：
3.5
通讯作者：
K. Lerch
中科院分区：
文献类型：
--
作者：
M. Beltramini;K. Lerch
金属硫蛋白是一类低锰含量、富含半胱氨酸的蛋白质，能结合异常大量的锌、镉和/或铜。这些蛋白在真核生物中普遍存在，据信它们在金属代谢中起着重要作用。相对于对金属硫蛋白结合位点的分子结构和理化性质的详细了解，其生物学功能仍是一个有争议的问题。除了金属解毒和储存功能[2]外，金属硫蛋白还被认为参与了金属向载金属蛋白的转移。特别是，金属硫蛋白中的锌离子被报道重新激活了一些锌依赖酶[2]。在此，我们研究了神经孢子菌铜金属硫蛋白[3]与神经孢子菌酪氨酸酶和癌血青素载脂蛋白之间的铜转移。重建效率与铜金属硫蛋白的氧化态密切相关。
Metallothioneins are a class of low-M r, cysteinerich proteins which bind unusually high amounts of Zn, Cd and/or Cu. These proteins occur ubiquitously in eukaryotic organisms where they are believed to play an important role in metal metabolism [1]. In contrast to the detailed knowledge on the molecular structure and the physical-chemical properties of the metal-binding sites of metallothioneins, their biological function is still a matter of controversy. Besides a metal detoxification and storage function [2], metallothioneins were also proposed to be involved in metal transfer to apometalloproteins. In particular, the zinc ions of metallothioneins were reported to reactivate a number of zinc-dependent enzymes [2]. Here, we have investigated the copper transfer between Neurospora copper metallothionein [3] and the apo-forms ofNeurospora tyrosinase and Carcinus hemocyanin. The reconstitution efficiency was found to be strongly dependent on the oxidation state of copper metallothionein.