Bell Stephen G, Vallee Bert L
The Inorganic Chemistry Laboratory, South Parks Road, Oxford, UK.
Chembiochem. 2009 Jan 5;10(1):55-62. doi: 10.1002/cbic.200800511.
Metallothioneins (MTs) were discovered more than 50 years ago and identified as low-molecular weight, sulfhydryl-rich proteins that were subsequently found to bind zinc predominantly. The binding of seemingly redox inactive zinc ions allows MT to play a central role in oxidoreductive cellular metabolism, cellular zinc distribution and homeostasis. In this interpretive study, we discuss the interaction of MT with physiologically relevant molecules and its effect on zinc-thiolate bonds. These interactions are linked to recent progress in the functional role of MT in cellular zinc transport, energy production, and protection of the organism against oxidative stress and neurodegenerative diseases.
金属硫蛋白(MTs)于50多年前被发现,并被鉴定为低分子量、富含巯基的蛋白质,随后发现其主要结合锌。看似无氧化还原活性的锌离子的结合使MT在氧化还原细胞代谢、细胞锌分布和体内平衡中发挥核心作用。在这项解释性研究中,我们讨论了MT与生理相关分子的相互作用及其对硫醇锌键的影响。这些相互作用与MT在细胞锌转运、能量产生以及机体对氧化应激和神经退行性疾病的保护作用方面的最新研究进展相关。