Enzyme-Based (Bio)Fuel Cells—Bilirubin Oxidase Use
| Autor: | T. Ruzgas |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Laccase
chemistry.chemical_classification Chemistry 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences Chloride Redox Combinatorial chemistry 0104 chemical sciences Catalysis Electron transfer Enzyme Biofuel medicine 0210 nano-technology Bilirubin oxidase medicine.drug |
| DOI: | 10.1016/b978-0-12-409547-2.13587-5 |
| Popis: | Discovered in 1981, bilirubin oxidase (BOD) became an important cathode enzyme in design of biofuel cells (BFCs). Substantial catalytic activity at neutral pH, minor inhibition by chloride ions and high-redox potential of the T1 copper site, being close to the redox potential of oxygen reduction to water, are the advantageous characteristics that distinguish this enzyme from other multicopper oxidases, for example, laccases, used in design of BFC cathodes. This article discusses the basic concept of BFCs and summarizes the achievements and limits which are reached by BFCs with focus on cathodes modified by BOD. Enzymatic cycle in homogeneous media and direct and mediated heterogeneous electron transfer of BOD are briefly summarized. |
| Databáze: | OpenAIRE |
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