Resonance raman spectra of "blue" copper proteins and the nature of their copper sites.
Resonance raman spectra of "blue" copper proteins and the nature of their copper sites.
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“蓝色”铜蛋白的共振拉曼光谱及其铜位点的性质。
DOI：
10.1021/ja00419a017
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发表时间：
1976
影响因子：
15
通讯作者：
P. Carey
中科院分区：
文献类型：
--
作者：
O. Siiman;N. Young;P. Carey
共鸣。用激光激发的~600 nm电子吸收带，在150-1700 cm“~(-1)范围内测量了5种”蓝色“铜蛋白[漆树胶、菠菜蓝蛋白、抗坏血酸铜蓝蛋白氧化酶和人铜蓝蛋白]的拉曼光谱。根据共振拉曼光谱和其他光谱和化学证据，提出“蓝”铜位具有扭曲的四配位结构，这是由于铜与一个半胱氨酸硫和三个氮原子结合而产生的，其中至少一个是酰胺氮。给出了与该结构有关的共振拉曼光谱的定性分子轨道描述。Stellacyanin的独特的共振拉曼光谱表明，它的“蓝色”铜位置与所研究的其他蛋白质中的那些显著不同。
Resonance. Raman spectra of five “blue” copper proteins {Rhus vernicifera stellacyanin and lacease, spinach plas-tocyanin, Cucúrbita pepo medullosa ascorbate oxidase, and human ceruloplasmin) were measured in the region 150to 1700 cm"" 1, using laser excitation into their~ 600-nm electronic absorptionbands. From the resonance Raman and other spectroscopic and chemical evidence, it is proposed that the “blue” copper site has a distorted four-coordinate structure arising from the bindingof copper to one cysteine sulfur and three nitrogen atoms, at least one of which is an amide nitrogen. A qualita-tive molecularorbital description relating the resonance Raman bands to the proposed structure is presented. The distinctive resonance Raman spectrum of stellacyanin suggested that its “blue” copper site differs markedly from those in the other proteins examined.