Supramolecular Linear Assemblies of Cytochrome b562 Immobilized on a Gold Electrode
Supramolecular Linear Assemblies of Cytochrome b562 Immobilized on a Gold Electrode
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DOI：
10.1007/s10904-012-9737-1
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发表时间：
2013-01-01
影响因子：
4
通讯作者：
Hayashi, Takashi
中科院分区：
文献类型：
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作者：
Kakikura, Yasuaki;Onoda, Akira;Hayashi, Takashi
通过连续的分子间血红素-血红素袋相互作用构建了蛋白质表面上含有化学修饰的血红素分子的细胞色素 b (562) (cyt b (562)) 的线性组装体，然后通过锚定在电极上的血红素分子固定到金电极上。通过电化学分析证实了 cyt b (562) 单位的积累。通过石英晶体微天平和原子力显微镜 (AFM) 分析估计每个组装体中蛋白质的平均数量约为 6 个单位。 AFM 清楚地将 cyt b (562) 单元的线性组件可视化为与电极表面垂直的棒状结构。
Linear assemblies of cytochrome b (562) (cyt b (562)) containing a chemically-modified heme molecule on the protein surface were constructed by successive intermolecular heme-heme pocket interactions and then immobilized onto a gold electrode via a heme molecule anchored on the electrode. The accumulation of the cyt b (562) units were confirmed by electrochemical analyses. The average number of proteins in each assembly was estimated to be about 6 units by quartz crystal microbalance and atomic force microscopy (AFM) analyses. The linear assemblies of the cyt b (562) units were clearly visualized by AFM as a rod-like architecture with a vertical orientation to the electrode surface.