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

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25 28 31 31 32 34 35 42 4 Peroxidases . . . . . . . . . . . . . . . . . . 2 Molybdenum-containing Enzymes . . . . . . . . . . . . Enzymes of the Xanthine Oxidase and Dimethyl Sulfoxide Reductase Families . . . . . . . . . Sulfite Oxidase . . . . . . . . . . . . . . . . . 51 53 6 Conclusion . . . . . . . . . . . . . . . . . . 56 References . . . . . . . . . . . . . . . . . . . . 57 . . . . . . . .

The reason is found in the structure of the enzyme. To ensure high selectivity towards its substrate the catalytic center is deeply buried in the polypeptide, and thus it is almost impossible to transfer electrons directly to or from an electrode without any conformational change. 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).

2 Cytochrome c Cytochrome c (Cyt c ) is a dimeric heme protein found in phototropic, sulfur oxidizing and denitrifying bacteria [80]. The heme moiety is bound to two cysteins, similar to the binding found in mitochondrial Cyt c. However, the iron atom of Cyt c is mainly high spin pentacoordinated. The sixth ligand site of ferrous Cyt c is deeply buried within the protein and closely surrounded by aromatic and hydrophobic amino acid residues, restricting access to exogenous compounds except to small molecules such as carbon monoxide and nitric oxide [81].

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