Xu Yanxia, Hu Chengguo, Hu Shengshui
College of chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Bioelectrochemistry. 2008 Apr;72(2):135-40. doi: 10.1016/j.bioelechem.2008.01.002. Epub 2008 Jan 7.
A novel approach that uses nature biological tissues, fish blood, for the study of the direct electron-transfer of hemoglobin and its catalytic activity for H(2)O(2) and NO(2)(-) is observed. The direct electron-transfer of hemoglobin in red blood cells in fish blood on glassy carbon electrode was observed for the first time. By simply casting fish blood on GC electrode surface and being air-dried, a pair of well-defined redox peaks for HbFe (III)/HbFe (II) appeared at about -0.36 V (vs SCE) at the fish blood film modified GCE in a pH 7.0 phosphate buffer solution. Ultraviolet visible (UV/VIS) characterization and the enhancement of the redox response of Hb by adding pure Hb in fish blood suggested that Hb preserved the native second structures in the fish blood film. Optical micrographs showed that the RBCs retained its integrity in blood. Hb in blood/GCE maintained its activity and could be used to electrocatalyze the reduction H(2)O(2) and NO(2)(-).
观察到一种新方法，即使用天然生物组织鱼血来研究血红蛋白的直接电子转移及其对H₂O₂和NO₂⁻的催化活性。首次观察到鱼血中红细胞内血红蛋白在玻碳电极上的直接电子转移。通过简单地将鱼血浇铸在玻碳电极表面并风干，在pH 7.0的磷酸盐缓冲溶液中，鱼血膜修饰的玻碳电极上出现了一对定义明确的HbFe(III)/HbFe(II)氧化还原峰，峰电位约为-0.36 V（相对于饱和甘汞电极）。紫外可见（UV/VIS）表征以及通过在鱼血中添加纯血红蛋白增强血红蛋白的氧化还原响应表明，血红蛋白在鱼血膜中保留了天然二级结构。光学显微镜照片显示红细胞在血液中保持其完整性。血液/玻碳电极中的血红蛋白保持其活性，可用于电催化还原H₂O₂和NO₂⁻。
