Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator.
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.
Fridman
V
V
University of Potsdam, Institute of Biochemistry and Molecular Physiology, Luckenwalde, Germany.
Wollenberger
U
U
Bogdanovskaya
V
V
Lisdat
F
F
Ruzgas
T
T
Lindgren
A
A
Gorton
L
L
Scheller
F W
FW
D002237:Carbohydrate Dehydrogenases / Q000378:metabolism*; D002475:Cellobiose / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism* / Q000502:physiology*; D004563:Electrochemistry; D004583:Electrons; D007700:Kinetics; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D020075:Phanerochaete / Q000201:enzymology; D011485:Protein Binding; D013053:Spectrophotometry
D003574:Cytochrome c Group; D002475:Cellobiose; D002237:Carbohydrate Dehydrogenases; C019859:cellobiose-quinone oxidoreductase; D010100:Oxygen