Conformational change in cytochrome P450 reductase adsorbed at a Au(110)-phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate.
Conformational change in cytochrome P450 reductase adsorbed at a Au(110)-phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate.
复制标题
与烟酰胺腺嘌呤二核苷酸磷酸盐相互作用诱导吸附在 Au(110)-磷酸盐缓冲液界面上的细胞色素 P450 还原酶的构象变化。
DOI：
10.1103/physreve.90.022708
复制
发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Smith CI
中科院分区：
文献类型：
--
作者：
Smith CI
在反射各向异性光谱（RAS）中观察到的细胞色素P450还原酶的单层吸附在Au（110）-电解质界面在0.056 V后，添加烟酰胺腺嘌呤二核苷酸磷酸的变化被解释在一个简单的模型中所产生的变化，在异咯嗪环的方向位于黄素单核苷酸结合域的蛋白质。该模型还解释了在RAS中观察到的变化，因为施加到Au（110）表面的电位是变化的，并表明，在RAS配置文件的依赖性的差异，吸附蛋白质对施加到电极上的电位在缺乏和存在的情况下，是可解释的，因为所施加的电位之间的竞争，以减少蛋白质和氧化它。
Changes observed in the reflection anisotropy spectroscopy (RAS) profiles of monolayers of cytochrome P450 reductase adsorbed at Au(110)–electrolyte interfaces at 0.056 V following the addition of nicotinamide adenine dinucleotide phosphateare explained in terms of a simple model as arising from changes in the orientation of an isoalloxazine ring located in the flavin mononucleotide binding domain of the protein. The model also accounts for the changes observed in the RAS as the potential applied to the Au(110) surface is varied and suggests that differences in the dependence of the RAS profile of the adsorbed protein on the potential applied to the electrode in the absence and presence ofare explicable as arising from a competition between the applied potential acting to reduce the protein and theto oxidize it.