High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins
High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins
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DOI：
10.1021/ac990947n
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发表时间：
2000-01-01
影响因子：
7.4
通讯作者：
Tao, NJ
中科院分区：
文献类型：
--
作者：
Boussaad, S;Pean, J;Tao, NJ
迄今为止，表面等离子体共振（SPR）光谱通过固定在表面上的配体的特定结合来识别分子。我们在这里证明：高分辨率多波长SPR技术可以测量分子的电子状态，从而允许直接识别分子。利用这种新能力，我们研究了固定在修饰金电极上的细胞色素c的氧化态和还原态的电子和构象差异。当入射光的波长远离蛋白质的光学吸收带时，当蛋白质从氧化态切换到还原态时，由于构象变化，共振角减少了0.008度。当波长调到吸收波段时，共振角在吸收峰的波长处振荡，这提供了蛋白质的电子特征。
To date, surface plasmon resonance (SPR) spectroscopy identifies molecules via specific bindings with their ligands immobilized on a surface. We demonstrate here that: a high-resolution multiwavelength SPR technique can measure the electronic states of the molecules and thus allow direct identification of the molecules. Using this new capability, we have studied the electronic and conformational differences between the oxidized and reduced states of cytochrome c immobilized on a modified gold electrode. When the wavelength of the incident light is far away from the optical absorption bands of the protein, a similar to 0.008 degrees decrease in the resonance angle, due to a conformational change, occurs as the protein is switched from the oxidized to reduced states. When the wavelength is tuned to the absorption bands, the resonance angle oscillates at the wavelengths of the absorption peaks, which provides electronic signatures of the protein.