The ability to catalyse an electrode reaction via direct (mediatorless) electron transfer has been demonstrated for a number of redox enzymes. In the case of mediatorless electron transfer, the electron is transferred directly from the electrode to the substrate molecule via the active site of the enzyme, or vice versa. The electron itself is the second substrate for the reaction. An important point characterizing bioelectrocatalysis is the catalytic removal of the reaction over-voltage. Therefore the enzyme attached to the electrode is able to catalyse electrode reaction and forms a ‘molecular transducer’. The substrate can be detected by potentiometric measurement of the removal of reaction over-voltage. The enzyme laccase is able to catalyse the reaction of oxygen electroreduction. Therefore a laccase molecular layer attached to the electrode surface forms an oxygen transducer. The formation of the layer results in a change of the electrocatalytic feature of the electrode. Laccase label coupled with either ligand or receptor allows the detection of ligand-receptor complex formation/dissociation on the electrode surface. The detection is virtually reagentless. The substrates for the reaction are molecular oxygen and the electron itself. Numerous reagentless immunosensors of different formats (competitive, displacement and sandwich) have been developed, as well as the reagentless detection system for immunofiltration/immunochromatography.
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February 2000
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Conference Article|
February 01 2000
Direct electron transfer catalysed by enzymes: application for biosensor development
A. Ghindilis
A. Ghindilis
*SynectiQ Corporation, Denville, NJ 07834, U.S.A.
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Publisher: Portland Press Ltd
Received:
September 09 1999
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2000 Biochemical Society
2000
Biochem Soc Trans (2000) 28 (2): 84–89.
Article history
Received:
September 09 1999
Citation
A. Ghindilis; Direct electron transfer catalysed by enzymes: application for biosensor development. Biochem Soc Trans 1 February 2000; 28 (2): 84–89. doi: https://doi.org/10.1042/bst0280084
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