Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator. (February 2000)

• Record Type: Journal Article
• Authors: Fridman, V.; Wollenberger, U.; Bogdanovskaya, V.; Lisdat, F.; Ruzgas, T.; Lindgren, A.; Gorton, L.; Scheller, F. W.
• Is Part Of: Biochemical Society transactions. Volume 28:Number 2(2000)
• Page Start: 63
• Page End: 70
• Publication Date: 2000-02
• Subjects: cyt, cytochrome -- CDH, cellobiose dehydrogenase -- MUA, 11-mercaptoundecanoic acid -- PQQ, pyrroloquinoline quinone; protein electochemistry; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0280063
• Languages: English
• ISSNs: 0300-5127

Abstract

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.