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By Reinhard Renneberg, Dorothea Pfeiffer, Fred Lisdat (auth.), Reinhard Renneberg, Fred Lisdat (eds.)

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Extra resources for Biosensing for the 21st Century

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1 The Role of the Interface For an effective bioelectric contact, the surface of the electrode, the material and pretreatment are of critical importance. The most successful electrodes are noble metal modified with various adsorbates and carbon materials and metal oxides that have natural surface functionalities. Self-assembling monolayers (SAM) of functionalized thiols on gold, polyelectrolyte and surfactant films on carbon, electron-transfer promoters in connection with various electrode material and metal oxides were shown to be suitable tools [2, 19, 22–27].

The enzymes capable of being in direct contact (without additional redox relays) with electrodes are those proteins that have protein interaction partners. Examples of such enzymes interacting with proteins are Cyt c peroxidase (CCP) and Cyt c, Cyt c3 and azurin, and CYP101 and putidaredoxin (Table 1). If the electrode is designed to resemble the surface characteristics of the protein (put simply, the net charge or hydrophobicity) the enzyme may bind to such a surface without dramatic structural changes and if the distance between the redox center and the electrode is low enough direct electrochemistry may be observed [63].

Abstract Electrochemistry using direct electron transfer between an electrode and a protein or an enzyme has developed into a means for studying biological redox reactions and for bioanalytics, biosynthesis and bioenergetics. This review summarizes recent work on direct protein electrochemistry with special emphasis on our results in bioelectrocatalysis using isolated enzymes and enzyme-protein couples.

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