Reconstitution of apo-glucose oxidase on nitrospiropyran and FAD mixed monolayers on gold electrodes: Photostimulation of bioelectrocatalytic features of the biocatalyst

Ron Blonder, Itamar Willner*, Andreas F. Bückmann

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

66 Scopus citations

Abstract

N6-(2-Aminoethyl)-FAD is covalently linked to a thioctic acid monolayer associated with an Au-electrode. The surface coverage of the FAD units is 2.2 x 10-11 mol cm-2. Apo-glucose oxidase (apo-GOx) reconstituted onto the FAD monolayer, yields a bioelectrocatalytically active enzyme layer, GOx, at a surface coverage of 2 x 10-12 mol cm-2. In the presence of N-dimethyl- 2-aminoethyl ferrocene (I) as diffusional electron mediator, the enzyme electrode stimulates the bioelectrocatalyzed oxidation of glucose. A photoisomerizable nitrospiropyran-FAD mixed monolayer is assembled on an Au- electrode. The surface coverage of the FAD units is 2 x 10-11 tool cm- 2, and the molar ratio of the nitrospiropyran and FAD units is 3:4. Reconstitution of apo-GOx onto the FAD sites of the photoisomerizable nitrospiropyran-FAD mixed monolayer yields a photoswitchable enzyme electrode for the light-stimulated oxidation of glucose in the presence of I as electron mediator. The photoswitchable properties of the enzyme electrode originate from the electrostatic repulsion of the positively charged electron mediator from the electrode interface. The GOx-reconstituted-monolayer electrode represents an optobioelectronic assembly for the amplified amperometric transduction of photonic signals recorded by the photoisomerizable monolayer.

Original languageEnglish
Pages (from-to)9335-9341
Number of pages7
JournalJournal of the American Chemical Society
Volume120
Issue number36
DOIs
StatePublished - 16 Sep 1998

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