尿素和乙酸对极酸性pH条件下高铁肌红蛋白血红素轴向配位结构的影响。
Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH.
作者信息
Droghetti Enrica, Sumithran Suganya, Sono Masanori, Antalík Marián, Fedurco Milan, Dawson John H, Smulevich Giulietta
机构信息
Dipartimento di Chimica, Università di Firenze, Via della Lastruccia 3, I-50019 Sesto Fiorentino (FI), Italy.
出版信息
Arch Biochem Biophys. 2009 Sep;489(1-2):68-75. doi: 10.1016/j.abb.2009.07.008. Epub 2009 Jul 19.
Abstract
The heme iron coordination of ferric myoglobin (Mb) in the presence of 9.0M urea and 8.0M acetic acid at acidic pH values has been probed by electronic absorption, magnetic circular dichroism and resonance Raman spectroscopic techniques. Unlike Mb at pH 2.0, where heme is not released from the protein despite the acid denaturation and the loss of the axial ligand, upon increasing the concentration of either urea or acetic acid, a spin state change is observed, and a novel, non-native six-coordinated high-spin species prevails, where heme is released from the protein.
摘要
在酸性pH值条件下，利用电子吸收光谱、磁圆二色光谱和共振拉曼光谱技术，对存在9.0M尿素和8.0M乙酸时的高铁肌红蛋白（Mb）的血红素铁配位情况进行了探究。与pH 2.0时的Mb不同，尽管发生了酸变性且轴向配体丢失，但血红素并未从蛋白质中释放出来。随着尿素或乙酸浓度的增加，会观察到自旋态变化，并且一种新型的、非天然的六配位高自旋物种占主导，此时血红素从蛋白质中释放出来。
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