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Electrochemical investigation of cellobiose dehydrogenase from new fungal sources on Au electrodes

Stoica, Leonard LU ; Dimcheva, N; Haltrich, D; Ruzgas, Tautgirdas LU and Gorton, Lo LU (2005) In Biosensors & Bioelectronics 20(10). p.2010-2018
Abstract
Following previous electrochemical investigations of cellobiose dehydrogenase (CDH), the present investigation reports on the initial screening of the electrochemistry of three new CDHs, two from the white rot basidiomycetes Trametes villosa and Phanerochaete sordida and one from the soft rot ascomycete Myriococcum thermophilum, for their ability to directly exchange electrons with 10 different alkanethiol-modified Au electrodes. Direct electron transfer (DET) between the enzymes and some of the modified Au electrodes was shown, both, in the presence and in the absence of cellobiose. However, the length and the head functionality of the alkanethiols drastically influenced the efficiency of the DET reaction and also influenced the effect of... (More)
Following previous electrochemical investigations of cellobiose dehydrogenase (CDH), the present investigation reports on the initial screening of the electrochemistry of three new CDHs, two from the white rot basidiomycetes Trametes villosa and Phanerochaete sordida and one from the soft rot ascomycete Myriococcum thermophilum, for their ability to directly exchange electrons with 10 different alkanethiol-modified Au electrodes. Direct electron transfer (DET) between the enzymes and some of the modified Au electrodes was shown, both, in the presence and in the absence of cellobiose. However, the length and the head functionality of the alkanethiols drastically influenced the efficiency of the DET reaction and also influenced the effect of pH on the biocatalyfic/redox currents, suggesting the importance of structural/sequence differences between these CDH enzymes. In this respect, the white rot CDHs exhibit excellent biocatalytic and redox currents, whereas for the soft rot CDH the DET communication is much less efficient. Cyclic voltammograms indicate that the heme domain of the CDHs is the part of the enzymes that most readily exchanges electrons with the electrode. However, for R sordida CDH on 11-mercaptoundecanol or dithiopropionic acid-modified Au electrodes, a second voltammetric wave was noticed suggesting that for some orientations of the enzyme, DET communication with the FAD cofactor can also be obtained. (c) 2004 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biosensors & Bioelectronics
volume
20
issue
10
pages
2010 - 2018
publisher
Elsevier
external identifiers
  • wos:000227845700016
  • pmid:15741070
  • scopus:14644411719
ISSN
1873-4235
DOI
10.1016/j.bios.2004.09.018
language
English
LU publication?
yes
id
4da06f58-6abf-46a1-a1af-d78a387f5df6 (old id 151093)
date added to LUP
2007-06-28 08:49:06
date last changed
2017-09-24 04:28:08
@article{4da06f58-6abf-46a1-a1af-d78a387f5df6,
  abstract     = {Following previous electrochemical investigations of cellobiose dehydrogenase (CDH), the present investigation reports on the initial screening of the electrochemistry of three new CDHs, two from the white rot basidiomycetes Trametes villosa and Phanerochaete sordida and one from the soft rot ascomycete Myriococcum thermophilum, for their ability to directly exchange electrons with 10 different alkanethiol-modified Au electrodes. Direct electron transfer (DET) between the enzymes and some of the modified Au electrodes was shown, both, in the presence and in the absence of cellobiose. However, the length and the head functionality of the alkanethiols drastically influenced the efficiency of the DET reaction and also influenced the effect of pH on the biocatalyfic/redox currents, suggesting the importance of structural/sequence differences between these CDH enzymes. In this respect, the white rot CDHs exhibit excellent biocatalytic and redox currents, whereas for the soft rot CDH the DET communication is much less efficient. Cyclic voltammograms indicate that the heme domain of the CDHs is the part of the enzymes that most readily exchanges electrons with the electrode. However, for R sordida CDH on 11-mercaptoundecanol or dithiopropionic acid-modified Au electrodes, a second voltammetric wave was noticed suggesting that for some orientations of the enzyme, DET communication with the FAD cofactor can also be obtained. (c) 2004 Elsevier B.V. All rights reserved.},
  author       = {Stoica, Leonard and Dimcheva, N and Haltrich, D and Ruzgas, Tautgirdas and Gorton, Lo},
  issn         = {1873-4235},
  language     = {eng},
  number       = {10},
  pages        = {2010--2018},
  publisher    = {Elsevier},
  series       = {Biosensors & Bioelectronics},
  title        = {Electrochemical investigation of cellobiose dehydrogenase from new fungal sources on Au electrodes},
  url          = {http://dx.doi.org/10.1016/j.bios.2004.09.018},
  volume       = {20},
  year         = {2005},
}