蓝色铜氧化酶铜蓝蛋白中2型铜的配位环境与氟化物结合
Coordination environment and fluoride binding of type 2 copper in the blue copper oxidase ceruloplasmin.
作者信息
Dawson J H, Dooley D M, Gray H B
出版信息
Proc Natl Acad Sci U S A. 1978 Sep;75(9):4078-81. doi: 10.1073/pnas.75.9.4078.
Abstract
The electron paramagnetic resonance (EPR) spectra of the blue copper oxidase ceruloplasmin [ferroxidase, iron (II):oxygen oxidoreductase, EC 1.16.3.1] and of a derivative having the type I (blue) copper centers reversibly bleached are reported. The EPR spectrum of bleached ceruloplasmin has a seven-line superhyperfine structure in the g : formula: (see text) region that is attributed to the presence of three nitrogen-donor type 2 copper ligands. The EPR data suggest further that the type 2 copper in ceruloplasmin possesses a tetragonal coordination gometry. In the presence of varying amounts of fluoride, superhyperfine splitting patterns in the g : formula: (see text) region of both ceruloplasmin derivatives indicate that a maximum of two fluorides may be bound to the type 2 copper.
摘要
报道了蓝铜氧化酶铜蓝蛋白[铁氧化酶，铁（II）：氧氧化还原酶，EC 1.16.3.1]及其具有可逆漂白的I型（蓝色）铜中心的衍生物的电子顺磁共振（EPR）光谱。漂白铜蓝蛋白的EPR光谱在g：公式：（见正文）区域具有七线超超精细结构，这归因于存在三个氮供体2型铜配体。EPR数据进一步表明，铜蓝蛋白中的2型铜具有四方配位几何结构。在存在不同量氟化物的情况下，两种铜蓝蛋白衍生物在g：公式：（见正文）区域的超超精细分裂模式表明，最多两个氟化物可能与2型铜结合。
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