Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator

被引:30
作者
Fridman, V
Wollenberger, U
Bogdanovskaya, V
Lisdat, F
Ruzgas, T
Lindgren, A
Gorton, L
Scheller, FW
机构
[1] Univ Potsdam, Inst Biochem & Mol Physiol, D-14943 Luckenwalde, Germany
[2] Russian Acad Sci, Inst Electrochem, Moscow 117071, Russia
[3] Lund Univ, Dept Analyt Chem, SE-22100 Lund, Sweden
关键词
protein electochemistry;
D O I
10.1042/bst0280063
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 accepters, 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.
引用
收藏
页码:63 / 70
页数:8
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