Reconstitution of apo-glucose dehydrogenase on pyrroloquinoline quinone-functionalized au nanoparticles yields an electrically contacted biocatalyst.
An electrically contacted glucose dehydrogenase ( GDH) enzyme electrode is fabricated by the reconstitution of the apo- GDH on pyrroloquinoline quinone (PQQ)-functionalized Au nanoparticles (Au-NPs), 1.4 nm, associated with a Au electrode. The Au-NPs functionalized with a single amine group were attached to the Au surface by 1,4-benzenedithiol bridges, and PQQ was covalently linked to the Au-NPs. The apo- GDH was then reconstituted on the PQQ cofactor sites. The surface coverage of GDH corresponded to 1.4 x 10(-12) mol cm(-2). The reconstituted enzyme revealed direct electrical contact with the electrode surface, and the bioelectrocatalytic oxidation of glucose occurred with a turnover number of 11,800 s(-1). In contrast, a system that included the covalent attachment of GDH to the PQQ-Au-NPs monolayer in a random, nonaligned, configuration revealed lack of electrical communication between the enzyme and the electrode, albeit the enzyme existed in a bioactive structure. The bioelectrocatalytic function of the later system was, however, activated by the diffusional electron mediator 2,6-dichlorophenol-indophenol. The results imply that the alignment of GDH on a Au-NP through the reconstitution process leads to an electrically contacted enzyme-electrode, where the Au-NP acts as a charge-transfer mediator.[1]References
- Reconstitution of apo-glucose dehydrogenase on pyrroloquinoline quinone-functionalized au nanoparticles yields an electrically contacted biocatalyst. Zayats, M., Katz, E., Baron, R., Willner, I. J. Am. Chem. Soc. (2005) [Pubmed]
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