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Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as
V Fridman1, U Wollenberger, V Bogdanovskaya
1University of Potsdam, Institute of Biochemistry and Molecular Physiology, Luckenwalde, Germany.
Abstract:
An important aspect of the cytochrome c electrochemistry is the possibility of coupling the 'heterogeneous reactions' with other redox enzymes. Cellobiose dehydrogenase, a 89170 Da glycoprotein that contains both FAD and a b-type haem as prosthetic groups, donates electrons to a number of acceptors, including cytochrome c. While haem b is surrounded mainly by acidic amino acids, cytochrome c displays positive charged lysine groups around the haem site. Thus a fast reaction between both proteins is explicable. In the presence of cellobiose, a catalytic current was observed, owing to the interaction of cellobiose dehydrogenase with electrostatically adsorbed cytochrome c. Adsorption of cytochrome c provides a technological model surface for vectorial electron transfer.