Solomon E I, Hare J W, Gray H B
Proc Natl Acad Sci U S A. 1976 May;73(5):1389-93. doi: 10.1073/pnas.73.5.1389.
Low temperature absorption, circular dichroism, and magnetic circular dichroism spectral studies of the blue copper proteins Rhus vernicifera stellacyanin, bean plastocyanin, and Pseudomonas aeruginosa azurin have been made. Low energy bands attributable to the d-d transitions 2B2 leads to 2E and 2B2 leads to 2B1 in a flattened tetrahedral (D 2d) copper-(II) center are observed in these proteins at about 5000 and 10,000 cm-1, respectively. The band positions accord well with ligand field calculations based on a tetrahedral structure that is distorted approximately 6 degrees toward a square plane. The ligands in this flattened tetrahedral coordination unit in bean plastocyanin are identified from various spectroscopic experiments as His-38, Cys-85, His-88, and a deprotonated peptide nitrogen (N) a few residues above His-38.
对蓝铜蛋白漆树漆蓝蛋白、豆类质体蓝素和铜绿假单胞菌天青蛋白进行了低温吸收、圆二色性和磁圆二色性光谱研究。在这些蛋白质中，分别在约5000和10000cm-1处观察到归因于扁平四面体（D2d）铜（II）中心中d-d跃迁2B2→2E和2B2→2B1的低能带。能带位置与基于向正方形平面扭曲约6度的四面体结构的配体场计算结果吻合良好。通过各种光谱实验确定，豆类质体蓝蛋白中这种扁平四面体配位单元中的配体为His-38、Cys-85、His-88以及His-38上方几个残基处的一个去质子化肽氮（N）。
