Lu Qing, Chen Xiaoxia, Wu Yunhua, Hu Shengshui
College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Biophys Chem. 2005 Aug 22;117(1):55-63. doi: 10.1016/j.bpc.2005.04.014.
Myoglobin (Mb), hemoglobin (Hb) and horseradish peroxidase (HRP) were incorporated in lecithin (PC) film on glassy carbon (GC) electrode by the method of vesicle-fusion. A pair of well-defined and quasi-reversible cyclic voltammetric peaks was obtained, which reflected the direct electron transfer of heme proteins. UV-Vis and reflectance absorption infrared (RAIR) spectroscopy showed that proteins in PC films remained at their secondary structure similar to their native states. Scanning electron microscopy (SEM) demonstrated the interaction between the proteins and PC would make the morphology of protein-PC films very different from the PC films alone. The immobilized proteins retained their biocatalytic activity to the reduction of NO and hydrogen peroxide, which provide the perspective to be the third generation sensors.
通过囊泡融合法将肌红蛋白（Mb）、血红蛋白（Hb）和辣根过氧化物酶（HRP）掺入玻碳（GC）电极上的卵磷脂（PC）膜中。获得了一对明确且准可逆的循环伏安峰，这反映了血红素蛋白的直接电子转移。紫外可见光谱和反射吸收红外（RAIR）光谱表明，PC膜中的蛋白质保持其与天然状态相似的二级结构。扫描电子显微镜（SEM）表明，蛋白质与PC之间的相互作用会使蛋白质-PC膜的形态与单独的PC膜有很大不同。固定化的蛋白质保留了其对NO和过氧化氢还原的生物催化活性，这为成为第三代传感器提供了前景。
