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Redox proteins perform diverse functions in cells, including electron transport, energy conversion, detoxification, enzymatic catalysis, signalling and gene regulation. The evolutionary optimised specificity and efficiency of enzymes has stimulated attempts to exploit these biocatalysts for a variety of technological applications. For example, enzymes are nowadays used to promote or to detect bio-specific interactions in biosensors (Karube, 1989). Several generations of low cost glucose oxidase–based biosensors are commercially available for monitoring the levels of glucose in diabetic individuals (Henning and Cunningham, 1998). Peroxidases are employed for biosensing of hydrogen peroxide and phenolic compounds, being relevant in environmental, pharmaceutical, clinical and industrial applications (Arya et al., 2009). Cytochromes P450 possess a high potential as biocatalysts for chemical synthesis although the transfer to biotechnological applications still represents a challenge (Leland and Clark, 1989; Todorovic et al., 2006; Cass, 2007). Understanding the enzymatic processes in cellular systems as well as in technological devices strongly depends on the knowledge of the molecular functioning of the enzymes. To this end specific approaches have been designed to explore the molecular processes of enzymes and redox proteins under conditions that reproduce most closely the physiological reaction. Membrane–bound redox proteins, such as respiratory chain electron transfer (ET) complexes, are incorporated into phospholipid bilayers, thus exerting their function in a hydrophobic environment under influence of the membrane potential. Small soluble metalloproteins that shuttle electrons between ET enzymes interact with the membranebound redox partners and the membrane itself. As a result of these interactions, the ET processes of electron shuttles are also subjected to strong electric fields at the membranesolution interface. These conditions are difficult to reproduce experimentally. In this respect, immobilization of redox proteins on biocompatible metal supports that function as 2

Immobilized Redox Proteins: Mimicking Basic Features of Physiological Membranes and Interfaces