Investigation of the mediated electron transfer mechanism of cellobiose dehydrogenase at cytochrome c-modified gold electrodes

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.

Ludwig, Roland (författare)
Haltrich, Dietmar (författare)
Gorton, LoLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)akem-lgo (författare)
Lisdat, Fred (författare)
Biokemi och StrukturbiologiCentrum för Molekylär Proteinvetenskap (creator_code:org_t)

Av författaren/redakt...: Sarauli, David; Ludwig, Roland; Haltrich, Dietma ...; Gorton, Lo; Lisdat, Fred

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