Biosensing for the 21st Century by Reinhard Renneberg, Dorothea Pfeiffer, Fred Lisdat (auth.),

Biosensing for the 21st Century by Reinhard Renneberg, Dorothea Pfeiffer, Fred Lisdat (auth.),

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

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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.

Hemoglobin and myoglobin) show reversible electron exchange at functionalized electrodes. A few of these proteins specifically interact with small signal molecules. d. d. d. d. d. d. d. DET 24 U. Wollenberger et al. Protein Electrodes with Direct Electrochemical Communication 25 cytochromes, hemoglobin and myoglobin for the analysis of superoxide anion [46–51], NO [52–55] and antioxidants [49, 56]. The reaction is a feature of the central iron atom. A number of studies reported the coupling of the heterogeneous electron transfer of a redox protein to complex biological electron-transfer reactions, in which the redox protein acts as vectorial redox mediator [3, 20, 21, 31, 57, 58] and electrochemistry provides the tool for examining both kinetics and mechanisms.

2 Molybdenum-containing Enzymes . . . . . . . . . . . . Enzymes of the Xanthine Oxidase and Dimethyl Sulfoxide Reductase Families . . . . . . . . . Sulfite Oxidase . . . . . . . . . . . . . . . . . 51 53 6 Conclusion . . . . . . . . . . . . . . . . . . 56 References . . . . . . . . . . . . . . . . . . . . 57 . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .

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