STRUCTURAL IMPLICATIONS DERIVED FROM ANALYSIS OF ELECTRON-PARAMAGNETIC RESONANCE-SPECTRA OF NATURAL AND ARTIFICIAL COPPER PROTEINS
STRUCTURAL IMPLICATIONS DERIVED FROM ANALYSIS OF ELECTRON-PARAMAGNETIC RESONANCE-SPECTRA OF NATURAL AND ARTIFICIAL COPPER PROTEINS
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DOI：
10.1016/0003-9861(74)90298-7
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发表时间：
1974-01-01
影响因子：
3.9
通讯作者：
BLUMBERG, WE
中科院分区：
文献类型：
--
作者：
PEISACH, J;BLUMBERG, WE
本文提出了一种将化学结构与EPR参数A_（？）对于具有相同连接原子的络合物，金属-配体络合物的电荷的减少使g减小，而使A增大。从这个分析中，我们可以得出结论，在人工铜蛋白和天然存在的非蓝色铜蛋白中，铜与氧和氮连接，但不与硫连接。本文提出了一种解释EPR变化的方法，这种变化发生在2型（非蓝色）铜位点的配体交换反应中，例如发生在漆酶中。
An extension of a method relating chemical structure to the EPR parameters A∥andg∥is presented. For complexes having the same atoms of ligation, a decrease in charge of the metal-ligand complex decreasesg∥and increases A∥. From this analysis, one concludes that in artificial copper proteins as well as in the naturally occurring nonblue copper proteins copper is ligated to oxygen and nitrogen but not to sulfur. A method is presented for the interpretation of EPR changes that occur with ligand exchange reactions at the Type 2 (nonblue) copper sites such as occur in laccase.