ANYL 447 |
| Oxidation state modulation of the redox enzymes is frequently required to elucidate their biomolecular function and application in various biotechnology devices. Producing and sustaining a well-defined protein redox state has been the common practical problem in modern bioresearch. For such purposes, chemical reduction by dithionite or ascorbate, and photochemical procedures employing dye in combination with an electron donor are traditionally used. However, both of these approaches have practical shortcomings. Electrochemistry was extensively utilized in mechanistic redox protein studies and their applications in biosensing over the last two decades. Interest in biomolecule solution spectroscopy methods has facilitated the application of the heterogeneous redox state control, typically dictated by sample purity requirements. We have shown that direct and sustainable heterogeneous electron transfer to redox proteins is achievable on semiconducting electrodes when their electronic properties are tuned to specific protein requirements. Semiconducting metal oxide electrodes serve as a capable platform for biomolecule thermodynamic and kinetic studies when combined with the optical spectroscopy detection. Spectroelectrochemical measurements of the redox biomolecules using the direct electron transfer between a solid electrode and solution species is particularly useful in mechanistic charge transfer investigations as they allow monitoring charge exchange between several biological redox partners. Distinctive capabilities of these measurements are demonstrated in studies of heme, iron-sulfur, di-oxo bridge, sulfhydryl, and flavin containing redox biomolecules.
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Analytical Approaches
1:30 PM-3:50 PM, Thursday, August 23, 2007 BCEC -- 104B, Oral
Division of Analytical Chemistry |