Investigation of the mediated electron transfer mechanism of cellobiose dehydrogenase at cytochrome c-modified gold electrodes
(2012) In Bioelectrochemistry 87. p.9-14- 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,... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3187457
- author
- Sarauli, David ; Ludwig, Roland ; Haltrich, Dietmar ; Gorton, Lo LU and Lisdat, Fred
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Cellobiose dehydrogenase, Direct electron transfer, Mediated electron, transfer, Cytochrome c, Immobilised enzyme
- in
- Bioelectrochemistry
- volume
- 87
- pages
- 9 - 14
- publisher
- Elsevier
- external identifiers
-
- wos:000309033000003
- scopus:84862857845
- pmid:21849263
- ISSN
- 1878-562X
- DOI
- 10.1016/j.bioelechem.2011.07.003
- language
- English
- LU publication?
- yes
- id
- 6a236a2e-330c-4dfa-a02c-9e47a27dc39f (old id 3187457)
- date added to LUP
- 2016-04-01 10:20:32
- date last changed
- 2023-09-28 00:14:41
@article{6a236a2e-330c-4dfa-a02c-9e47a27dc39f, 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.}}, author = {{Sarauli, David and Ludwig, Roland and Haltrich, Dietmar and Gorton, Lo and Lisdat, Fred}}, issn = {{1878-562X}}, keywords = {{Cellobiose dehydrogenase; Direct electron transfer; Mediated electron; transfer; Cytochrome c; Immobilised enzyme}}, language = {{eng}}, pages = {{9--14}}, publisher = {{Elsevier}}, series = {{Bioelectrochemistry}}, title = {{Investigation of the mediated electron transfer mechanism of cellobiose dehydrogenase at cytochrome c-modified gold electrodes}}, url = {{http://dx.doi.org/10.1016/j.bioelechem.2011.07.003}}, doi = {{10.1016/j.bioelechem.2011.07.003}}, volume = {{87}}, year = {{2012}}, }