Abstract
Direct electron transfer between redox proteins and metal electrodes has many advantages with respect to analytical applications. Hill and coworkers1 have pointed out the similarities between heterogeneous electron transfer reactions of proteins at electrodes and catalysis. The sequence of events at the electrode include: 1) diffusion of reactant protein to the electrode surface; 2) adsorption of the protein in an orientation suitable for electron transfer; 3) electron transfer; 4) dissociation of the protein from the electrode surface; and 5) diffusion of the protein away from the surface. If all these requirements are not met, well behaved redox activity will not be observed. There have been various approaches to accomplishing reversible redox reactions in proteins based upon these requirements. Hill and coworkers have focused on the second step and have shown by their elegant promoter studies that the correct orientation of the protein at the electrode is crucial for rapid electron transfer. Others have utilized mediator-type electrodes or chemically modified proteins2.
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© 1988 Plenum Press, New York
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Holt, R.E., Cotton, T.M. (1988). Serrs as a Probe of Electrode Processes: Interaction of Glucose Oxidase and Fad at Silver Electrodes. In: Dryhurst, G., Niki, K. (eds) Redox Chemistry and Interfacial Behavior of Biological Molecules. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9534-2_16
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DOI: https://doi.org/10.1007/978-1-4615-9534-2_16
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