Advanced

Investigation of the pH-Dependent Electron Transfer Mechanism of Ascomycetous Class II Cellobiose Dehydrogenases on Electrodes

Harreither, Wolfgang; Nicholls, Peter; Sygmund, Christoph; Gorton, Lo LU and Ludwig, Roland (2012) In Langmuir 28(16). p.6714-6723
Abstract
Cellobiose dehydrogenase (CDH) is capable of direct electron transfer (DET) on various carbon and thiol-modified gold electrodes. As a result, these systems have been utilized as biocatalyst in biosensors and biofuel cell anodes. Class I CDHs, from basidiomycetous fungi, are highly specific to cellulose or lactose, and DET is only observed at pH values below 5.5. To extend the applicability of CDH-based electrodes, the catalytic properties and the behavior on electrode surfaces of ascomycetous class II CDHs from Chaetomium attrobrunneum, Corynascus thermophilus, Dichomera saubinetii, Hypoxylon haematostroma, Neurospora crassa, and Stachybotrys bisbyi were investigated. We found that class II CDHs have diverse properties but generally show... (More)
Cellobiose dehydrogenase (CDH) is capable of direct electron transfer (DET) on various carbon and thiol-modified gold electrodes. As a result, these systems have been utilized as biocatalyst in biosensors and biofuel cell anodes. Class I CDHs, from basidiomycetous fungi, are highly specific to cellulose or lactose, and DET is only observed at pH values below 5.5. To extend the applicability of CDH-based electrodes, the catalytic properties and the behavior on electrode surfaces of ascomycetous class II CDHs from Chaetomium attrobrunneum, Corynascus thermophilus, Dichomera saubinetii, Hypoxylon haematostroma, Neurospora crassa, and Stachybotrys bisbyi were investigated. We found that class II CDHs have diverse properties but generally show a lower substrate specificity than class I CDHs by converting also glucose and maltose. Intramolecular electron transfer (JET) and DET at neutral and alkaline pH were observed and elucidated by steady-state kinetics, pre-steady-state kinetics, and electrochemical measurements. The CDHs ability to interact with the electron acceptor cytochrome c and to communicate with electrode surfaces through DET at various pH conditions was used to classify the investigated enzymes. In combination with stopped-flow measurements, a model for the kinetics of the pH-dependent JET is developed. The efficient glucose turnover at neutral/alkaline pH makes some of these new CDHs potential candidates for glucose biosensors and biofuel cell anodes, (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
28
issue
16
pages
6714 - 6723
publisher
The American Chemical Society
external identifiers
  • wos:000303091300025
  • scopus:84860197665
ISSN
0743-7463
DOI
10.1021/la3005486
language
English
LU publication?
yes
id
0663e909-4dfa-4939-82d4-999b64f6fd4d (old id 2566395)
date added to LUP
2012-06-01 13:32:51
date last changed
2017-09-24 03:01:48
@article{0663e909-4dfa-4939-82d4-999b64f6fd4d,
  abstract     = {Cellobiose dehydrogenase (CDH) is capable of direct electron transfer (DET) on various carbon and thiol-modified gold electrodes. As a result, these systems have been utilized as biocatalyst in biosensors and biofuel cell anodes. Class I CDHs, from basidiomycetous fungi, are highly specific to cellulose or lactose, and DET is only observed at pH values below 5.5. To extend the applicability of CDH-based electrodes, the catalytic properties and the behavior on electrode surfaces of ascomycetous class II CDHs from Chaetomium attrobrunneum, Corynascus thermophilus, Dichomera saubinetii, Hypoxylon haematostroma, Neurospora crassa, and Stachybotrys bisbyi were investigated. We found that class II CDHs have diverse properties but generally show a lower substrate specificity than class I CDHs by converting also glucose and maltose. Intramolecular electron transfer (JET) and DET at neutral and alkaline pH were observed and elucidated by steady-state kinetics, pre-steady-state kinetics, and electrochemical measurements. The CDHs ability to interact with the electron acceptor cytochrome c and to communicate with electrode surfaces through DET at various pH conditions was used to classify the investigated enzymes. In combination with stopped-flow measurements, a model for the kinetics of the pH-dependent JET is developed. The efficient glucose turnover at neutral/alkaline pH makes some of these new CDHs potential candidates for glucose biosensors and biofuel cell anodes,},
  author       = {Harreither, Wolfgang and Nicholls, Peter and Sygmund, Christoph and Gorton, Lo and Ludwig, Roland},
  issn         = {0743-7463},
  language     = {eng},
  number       = {16},
  pages        = {6714--6723},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Investigation of the pH-Dependent Electron Transfer Mechanism of Ascomycetous Class II Cellobiose Dehydrogenases on Electrodes},
  url          = {http://dx.doi.org/10.1021/la3005486},
  volume       = {28},
  year         = {2012},
}