A molecular wire modified glassy carbon electrode for achieving direct electron transfer to native glucose oxidase |
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| Institution: | 1. Biosystems Technology, Institute of Applied Life Sciences, Technical University of Applied Sciences, 15745 Wildau, Germany;2. Technical University Darmstadt, Eduard-Zintl-Institute for Inorganic and Physical Chemistry, 64287 Darmstadt, Germany;1. State Key Laboratory of Advanced Metallurgy, University of Science and Technology Beijing, Beijing 100083, PR China;2. Beijing Institute of Radiation Medicine, Beijing 100850, PR China;1. Department of Inorganic Chemistry, Physical Chemistry and Electrochemistry, University “Politehnica” of Bucharest, 1-7 Polizu St., 011061, Bucharest, Romania;2. “Costin Nenitzescu” Department of Organic Chemistry, University “Politehnica” of Bucharest, 1-7 Polizu St., 011061, Bucharest, Romania;3. Advanced Polymer Materials Group, University “Politehnica” of Bucharest, 1-7 Polizu St., 011061, Bucharest, Romania;4. Department of Physics, University “Politehnica” of Bucharest, 313 Splaiul Independentei, 060042, Bucharest, Romania;5. Department of Organic Chemistry, Biochemistry and Catalysis, University of Bucharest, 4-12 Regina Elisabeta Av., 030016, Bucharest, Romania;6. Center for Surface Science and Nanotechnology, University “Politehnica” of Bucharest, 313 Splaiul Independentei, 060042, Bucharest, Romania |
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| Abstract: | Here we describe a strategy for achieving direct electron transfer to native glucose oxidase (GOx), an enzyme in which the redox active centre is buried deep within the glycoprotein. To achieve this a glassy carbon electrode is modified with a mixed monolayer of 4-carboxyphenyl and a 20 Å long oligo(phenylethynyl) molecular wire (MW), assembled from the respective aryl diazonium salts. Subsequently GOx is adsorbed to the interface, followed by covalent attachment. The redox chemistry of the active centre of glucose oxidase, flavin adenine dinucleotide, was observed at an E1/2 of –443 mV (vs. Ag|AgCl). The enzyme was shown to retain its activity. Most importantly, in the absence of oxygen the electrode was still able to biocatalytically turn over glucose at ?400 mV, thereby demonstrating that the enzyme was being recycled back to its catalytically active oxidized form from its inactive reduced form. The rate of enzyme turnover was 1.1 s?1. |
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