Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces Ordered multilayers of cytochrome P450 reductase
Ordered multilayers of cytochrome P450 reductase adsorbed at Au(110)/phosphate buffer interfaces Ordered multilayers of cytochrome P450 reductase
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吸附在 Au(110)/磷酸盐缓冲液界面的有序多层细胞色素 P450 还原酶 有序多层细胞色素 P450 还原酶
DOI：
10.1002/pssb.201451221
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Smith C
中科院分区：
文献类型：
--
作者：
Smith C
细胞色素P450还原酶P499 C的突变形式的双层和多层在吸附于Au（110）/磷酸盐缓冲液界面时形成有序结构。反射各向异性光谱（RAS）表明，程度的顺序增加的层数和光学偶极子，有助于从双层观察到的RAS配置文件中的平面是定向垂直于表面和沿着的Au（110）表面的主轴之一。Au（110）底物和蛋白质对组合系统的RAS分布的贡献显示出对施加到Au（110）电极的电势的相反依赖性。从吸附的多层膜观察到的RAS分布主要由蛋白质的贡献。
Bilayers and multilayers of a mutated form of cytochrome P450 reductase, P499C, form ordered structures when adsorbed at Au(110)/phosphate buffer interfaces. Reflection anisotropy spectroscopy (RAS) indicates that the degree of order increases with the number of layers and that the optical dipoles that contribute to the RAS profiles observed from the bilayer lie in planes that are oriented vertical to the surface and along one of the principal axes of the Au(110) surface. The contribution of the Au(110) substrate and the protein to the RAS profiles of the combined systems show an opposite dependence on the potential applied to the Au(110) electrode. The RAS profile observed from an adsorbed multilayer is dominated by the contribution from the protein.