Bielli P, Calabrese L
Institute of Microbiology and Genetics, Vienna Biocenter, University of Vienna, Austria.
Cell Mol Life Sci. 2002 Sep;59(9):1413-27. doi: 10.1007/s00018-002-8519-2.
Specialised copper sites have been recruited during evolution to provide long-range electron transfer reactivity and oxygen binding and activation in proteins destined to cope with oxygen reactivity in different organisms. Ceruloplasmin is an ancient multicopper dase evolved to insure a safe handling of oxygen in some metabolic pathways of vertebrates. The presently available knowledge of its structure provides a glimpse of its plasticity, revealing a multitude of binding sites that point to an elaborate mechanism of multifunctional activity. Ceruloplasmin represents an example of a 'moonlighting' protein that overcomes the one gene-one structure-one function concept to follow the changes of the organism in its physiological and pathological conditions.
在进化过程中,专门的铜位点被招募来提供远程电子转移反应性以及在注定要应对不同生物体中氧反应性的蛋白质中进行氧结合和激活。铜蓝蛋白是一种古老的多铜氧化酶,进化而来以确保在脊椎动物的某些代谢途径中安全处理氧气。目前关于其结构的现有知识让我们得以一窥其可塑性,揭示了众多结合位点,这表明存在一种复杂的多功能活性机制。铜蓝蛋白代表了一种“兼职”蛋白的例子,它打破了一个基因 - 一种结构 - 一种功能的概念,以适应生物体在生理和病理条件下的变化。