Title: Immobilization of flavins on electrode surfaces
Abstract: The covalent attachment of flavin cofactors to electron-conducting supports serves both as a probe of the spatial requirements for flavinapoenzyme association as well as a novel route for the development of cofactor-apoenzyme electrodes. In this work, a procedure is described for the apparent conversion of riboflavin, immobilized at position 8 to glassy carbon, to flavin mononucleotide (FMN) and then to immobilized flavin adenine dinucleotide (FAD). The attached materials were characterized electrochemically and coenzymatically. FAD serves as the cofactor for the enzyme glucose oxidase. Partial restoration of enzyme activity was achieved by incubation of the FAD-electrode with apoglucose oxidase. This is the first reported covalent coupling of a coenzymatically active flavin to an electrode through the flavin position 8 group.
Publication Year: 1986
Publication Date: 1986-03-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 15
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