The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Direct Electrochemistry and Electrocatalysis of Heme Proteins Entrapped in Agarose Hydrogel Films in Room-Temperature Ionic Liquids
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][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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Metadata
- Authors
- Wang, S.-F., Chen, T., Zhang, Z.-L., Shen, X.-C., Lu, Z.-X., Pang, D.-W., & Wong, K.-Y.
- Venue
- Langmuir
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-08-13
- Volume
- 21
- Issue
- 20
- Pages
- 9260-9266
- ISSN
- 0743-7463 (ISSN-L)
- 1520-5827
- OpenAlex
- W3151666537
- Cited by
- 348
- References
- 19
- FWCI
- 20.97
- Type
- journal article
- Language
- en
- Open access
- closed
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