Studies of the metal sites of copper proteins. Ligands of copper in hemocuprein.
Studies of the metal sites of copper proteins. Ligands of copper in hemocuprein.
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铜蛋白金属位点的研究。
DOI：
10.1021/bi00780a011
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发表时间：
1971
期刊：
影响因子：
2.9
通讯作者：
B. Mondovì
中科院分区：
文献类型：
--
作者：
G. Rotilio;A. Agrò;L. Calabrese;F. Bossa;P. Guerrieri;B. Mondovì
Giuseppe Rotilo，Alessandro Finazzi Ago，Lilia Calabrese，Francesco Bossa，PietroGuerrieri和Bruno Mondovi摘要：研究了不同条件下牛血红素的电子顺磁共振、光吸收和圆二色谱，以获得铜结合位置的信息。当蛋白质溶液的pH升高到11.5时，在蛋白质结合铜的电子顺磁共振谱上观察到了9条间距约为14G的超精细图谱。这一光谱可以用三到四个氮原子作为铜的配体来解释。通过降低pH值，完全恢复了原来的光谱。在吸收光谱和圆二色谱中观察到的平行变化也是可逆的。在pH为11.5时的圆二色谱显示了与中性pH时相同的椭圆度带的多样性，只是峰的相对强度发生了变化；这有力地支持了这一观点
Giuseppe Rotilio, Alessandro Finazzi Agro, Lilia Calabrese, Francesco Bossa, PietroGuerrieri, and Bruno Mondovi abstract: The electron paramagnetic resonance, optical absorption, and circular dichroism spectra of bovine erythrocuprein (hemocuprein) were studied under various conditions to obtain information on the copper binding site. When the pH of the protein solution was raised to pH 11.5, a super-hyperfine pattern of nine lines with spacing of about 14 G was observed in the electron paramagnetic resonance spectrum of the protein-bound copper. Thisspectrum can be accounted for by the presence of three to four nitrogen atoms as ligands of copper. The original spectrum was fully recovered by lowering the pH. Also the parallel changes noticed in the absorption and circular dichroism spectra were reversible. The circular dichroism spectrum at pH 11.5 displayed the same multiplicity of ellipticity bands as at neutral pH, only the relative intensity of thepeaks being changed; this strongly supports the idea that the