Comment on "Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids".
Comment on "Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids".
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DOI：
10.1021/la061336a
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发表时间：
2005-08
期刊：
影响因子：
--
通讯作者：
Z. Brusova;L. Gorton;E. Magner
中科院分区：
文献类型：
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作者：
Z. Brusova;L. Gorton;E. Magner
研究了包埋在琼脂糖凝胶膜中的血红素蛋白在室温离子液体1-丁基-3-甲基咪唑六氟磷酸盐（[bmim][PF 6]）中的电化学和电催化作用.紫外维斯光谱和红外光谱表明，血红素蛋白在琼脂糖膜中保持其天然结构。用原子力显微镜证实了血红蛋白在琼脂糖-二甲基甲酰胺膜中的均匀分布。循环伏安法表明，在[bmim][PF 6]中，血红素蛋白与玻碳电极之间的直接电子转移是准可逆的。血红蛋白，肌红蛋白，辣根过氧化物酶，细胞色素c，和过氧化氢酶的氧化还原电位被发现是更负比那些在水溶液中。这些血红素蛋白在[bmim][PF 6]的电荷转移系数和表观电子转移速率常数计算从峰-峰分离作为扫描速率的函数。血红素蛋白催化三氯乙酸的电还原。
The electrochemistry and electrocatalysis of a number of heme proteins entrapped in agarose hydrogel films in the room-temperature ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim][PF6]) have been investigated. UV−vis and FTIR spectroscopy show that the heme proteins retain their native structure in agarose film. The uniform distribution of hemoglobin in agarose−dimethylformamide film was demonstrated by atomic force microscopy. Cyclic voltammetry shows that direct electron transfer between the heme proteins and glassy carbon electrode is quasi-reversible in [bmim][PF6]. The redox potentials for hemoglobin, myoglobin, horseradish peroxidase, cytochrome c, and catalase were found to be more negative than those in aqueous solution. The charge-transfer coefficient and the apparent electron-transfer rate constant for these heme proteins in [bmim][PF6] were calculated from the peak-to-peak separation as a function of scan rate. The heme proteins catalyze the electroreduction of trichloroacet...