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鳟鱼血红蛋白组分IV的碳氧单氧基衍生物中质子偶联转变的圆二色性研究。

A circular dichroism study of the proton-linked transition in the carbomonoxy derivative of the hemoglobin component IV from trout.

作者信息

Ascoli F, Santucci R, Falcioni G, Brunori M

出版信息

Biochim Biophys Acta. 1983 Feb 15;742(3):565-7. doi: 10.1016/0167-4838(83)90274-1.

DOI:10.1016/0167-4838(83)90274-1
PMID:6301557
Abstract

Near ultraviolet and visible circular dichroism spectra of the carbomonoxy derivative of the hemoglobin component IV from trout Salmo irideus are pH-dependent in the range 6.2-7.8, and are affected by the presence of inositol hexaphosphate at pH 6.2. On the basis of previous studies, the spectral changes observed can be associated to the pH-dependent R4 leads to T4 transition occurring in the liganded protein. The CD spectra above 500 nm at low pH can be interpreted as due to release of the heme asymmetry in the T liganded conformation, in agreement with the movement of the iron toward the proximal histidine.

摘要

虹鳟鱼血红蛋白组分IV的碳氧单氧基衍生物的近紫外和可见圆二色光谱在6.2 - 7.8范围内依赖于pH值,并且在pH 6.2时受肌醇六磷酸的存在影响。根据先前的研究,观察到的光谱变化可能与配体蛋白中发生的依赖于pH的R4到T4转变有关。低pH下500 nm以上的圆二色光谱可以解释为是由于T配体构象中血红素不对称性的释放,这与铁向近端组氨酸的移动一致。

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引用本文的文献

1
Thermodynamic characterization of the allosteric transition in trout hemoglobin.鳟鱼血红蛋白变构转变的热力学特征
Eur Biophys J. 1986;13(4):245-9. doi: 10.1007/BF00260371.