Reconstitution of apo-glucose oxidase on nitrospiropyran and FAD mixed monolayers on gold electrodes:: Photostimulation of bioelectrocatalytic features of the biocatalyst
被引:58
作者:
Blonder, R
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机构:Hebrew Univ Jerusalem, Inst Chem, IL-91904 Jerusalem, Israel
N-6-(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). Ape-glucose oxidase (apo-GOx) reconstituted onto the FAD monolayer, yields a bioelectrocatalyticaIly 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) mol 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.