Construction of Uniform Monolayer- and Orientation-Tunable Enzyme Electrode by a Synthetic Glucose Dehydrogenase without Electron-Transfer Subunit via Optimized Site-Specific Gold-Binding Peptide Capable of Direct Electron Transfer
| Autor: | Hyunsoo Kang, Hyeryeong Lee, Yeongeun Kim, In Geol Choi, Yoo Seok Lee, Stacy Simai Reginald, Seungwoo Baek, In Seop Chang |
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| Rok vydání: | 2018 |
| Předmět: |
Enzyme complex
Materials science Enzyme electrode Electrons Peptide Biosensing Techniques 02 engineering and technology 010402 general chemistry 01 natural sciences Electron Transport Electron transfer Glucose dehydrogenase General Materials Science Electrodes chemistry.chemical_classification Glucose 1-Dehydrogenase Electron acceptor Enzymes Immobilized 021001 nanoscience & nanotechnology Combinatorial chemistry Electron transport chain 0104 chemical sciences Glucose chemistry Gold Peptides 0210 nano-technology Biosensor |
| Zdroj: | ACS Applied Materials & Interfaces. 10:28615-28626 |
| ISSN: | 1944-8252 1944-8244 |
| Popis: | Direct electron transfer (DET) between enzymes and electrodes is a key issue for practical use of bioelectrocatalytic devices as a bioenergy process, such as enzymatic electrosynthesis, biosensors, and enzyme biofuel cells. To date, based on the DET of bioelectrocatalysis, less than 1% of the calculated theoretical current was transferred to final electron acceptor due to energy loss at enzyme-electrode interface. This study describes the design and construction of a synthetic glucose dehydrogenase (GDH; α and γ subunits) combined with a gold-binding peptide at its amino or carboxy terminus for direct contact between enzyme and electrode. The fused gold-binding peptide facilitated stable immobilization of GDH and constructed uniform monolayer of GDH onto a Au electrode. Depending on the fused site of binding peptide to the enzyme complex, nine combinations of recombinant GDH proteins on the electrode show significantly different direct electron-transfer efficiency across the enzyme-electrode interface. The fusion of site-specific binding peptide to the catalytic subunit (α subunit, carboxy terminus) of the enzyme complex enabled apparent direct electron transfer (DET) across the enzyme-electrode interface even in the absence of the electron-transfer subunit (i.e., β subunit having cytochrome domain). The catalytic glucose oxidation current at an onset potential of ca. (-)0.46 V vs Ag/AgCl was associated with the appearance of an flavin adenine dinucleotide (FAD)/FADH |
| Databáze: | OpenAIRE |
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