Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids

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][PF(6)]) have been investigated. UV-vis and FTIR spectroscopy show that the heme proteins retain thei...

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Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1991. - 21(2005), 20 vom: 27. Sept., Seite 9260-6
Auteur principal: Wang, Sheng-Fu (Auteur)
Autres auteurs: Chen, Ting, Zhang, Zhi-Ling, Shen, Xin-Cheng, Lu, Zhe-Xue, Pang, Dai-Wen, Wong, Kwok-Yin
Format: Article
Langue:English
Publié: 2005
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Research Support, Non-U.S. Gov't Hemeproteins Hydrogels Water 059QF0KO0R Trichloroacetic Acid 5V2JDO056X Sepharose 9012-36-6 plus... tert-Butylhydroperoxide 955VYL842B
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245 1 0 |a Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids 
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500 |a CommentIn: Langmuir. 2006 Dec 19;22(26):11453-5. doi: 10.1021/la061336a. - PMID 17154639 
500 |a Citation Status MEDLINE 
520 |a 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][PF(6)]) 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][PF(6)]. The kinetic parameter I(max) (maximum current at saturation concentration of substrate) and the apparent K(m) (Michaelis-Menten constant) for the electrocatalytic reactions were evaluated 
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650 7 |a tert-Butylhydroperoxide  |2 NLM 
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700 1 |a Chen, Ting  |e verfasserin  |4 aut 
700 1 |a Zhang, Zhi-Ling  |e verfasserin  |4 aut 
700 1 |a Shen, Xin-Cheng  |e verfasserin  |4 aut 
700 1 |a Lu, Zhe-Xue  |e verfasserin  |4 aut 
700 1 |a Pang, Dai-Wen  |e verfasserin  |4 aut 
700 1 |a Wong, Kwok-Yin  |e verfasserin  |4 aut 
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