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Gewählte Publikation:

Sarauli, D; Ludwig, R; Haltrich, D; Gorton, L; Lisdat, F.
(2012): Investigation of the mediated electron transfer mechanism of cellobiose dehydrogenase at cytochrome c-modified gold electrodes.
Bioelectrochemistry. 2012; 87(3-4):9-14 FullText FullText_BOKU

Abstract:
The present study reports on the comparison of direct and mediated electron transfer pathways in the interaction of the fungal enzyme cellobiose dehydrogenase (CDH) with the redox protein cytochrome c (cyt c) immobilised at a modified gold electrode surface. Two types of CDHs were chosen for this investigation: a basidiomycete (white rot) CDH from Trametes villosa and a recently discovered ascomycete from the thermophilic fungus Corynascus thermophilus. The choice was based on the pH-dependent interaction of these enzymes with cyt c in solution containing the substrate cellobiose (CB). Both enzymes show rather similar catalytic behaviour at lower pH, dominated by a direct electron exchange with the electrode. With increasing pH, however, also cyt c-mediated electron transfer becomes possible. The pH-dependent behaviour in the presence and in the absence of cyt c is analysed and the potential reaction mechanism for the two enzymes with a different pH-behaviour is discussed. (c) 2011 Published by Elsevier B.V.
Autor/innen der BOKU Wien:
Haltrich Dietmar
Ludwig Roland
BOKU Gendermonitor:


Find related publications in this database (Keywords)
Cellobiose dehydrogenase
Direct electron transfer
Mediated electron transfer
Cytochrome c
Immobilised enzyme


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