Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/20879
Title: Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids
Authors: Wang, SF
Chen, T
Zhang, ZL
Shen, XC
Lu, ZX
Pang, DW
Wong, KY 
Issue Date: 2005
Source: Langmuir, 2005, v. 21, no. 20, p. 9260-9266 How to cite?
Journal: Langmuir 
Abstract: 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][PF 6]. 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][PF 6] were calculated from the peak-to-peak separation as a function of scan rate. The heme proteins catalyze the electroreduction of trichloroacetic acid and tert-butyl hydroperoxide in [bmim] [PF6]. The kinetic parameter Imax (maximum current at saturation concentration of substrate) and the apparent Km (Michaelis-Menten constant) for the electrocatalytic reactions were evaluated.
URI: http://hdl.handle.net/10397/20879
ISSN: 0743-7463
DOI: 10.1021/la050947k
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