Advanced

Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes

Ortiz, Roberto LU ; Matsumura, Hirotoshi LU ; Tasca, Federico LU ; Zahma, Kawah; Samejima, Masahiro; Igarashi, Kiyohiko; Ludwig, Roland and Gorton, Lo LU (2012) In Analytical Chemistry 84(23). p.10315-10323
Abstract
Cellobiose dehydrogenase (CDH) is a monomeric extracellular flavocytochrome composed of a catalytic dehydrogenase domain (DHCDH) containing flavin adenine dinucleotide (FAD), a cytochrome domain (CYTCDH) containing heme b, and a linker region connecting the two domains. In this work, the effect of deglycosylation on the electrochemical properties of CDH from Phanerochaete chrysosporium (PcCDH) and Ceriporiopsis subvermispora (CsCDH) is presented. All the glycosylated and deglycosylated enzymes show direct electron transfer (DET) between the CYTCDH and the electrode. Graphite electrodes modified with deglycosylated PcCDH (dPcCDH) and CsCDH (dCsCDH) have a 40-65% higher I-max value in the presence of substrate than electrodes modified with... (More)
Cellobiose dehydrogenase (CDH) is a monomeric extracellular flavocytochrome composed of a catalytic dehydrogenase domain (DHCDH) containing flavin adenine dinucleotide (FAD), a cytochrome domain (CYTCDH) containing heme b, and a linker region connecting the two domains. In this work, the effect of deglycosylation on the electrochemical properties of CDH from Phanerochaete chrysosporium (PcCDH) and Ceriporiopsis subvermispora (CsCDH) is presented. All the glycosylated and deglycosylated enzymes show direct electron transfer (DET) between the CYTCDH and the electrode. Graphite electrodes modified with deglycosylated PcCDH (dPcCDH) and CsCDH (dCsCDH) have a 40-65% higher I-max value in the presence of substrate than electrodes modified with their glycosylated counterparts. CsCDH trapped under a permselective membrane showed similar changes on gold electrodes protected by a thiol-based self-assembled monolayer (SAM), in contrast to PcCDH for which deglycosylation did not exhibit any different electrocatalytical response on SAM-modified gold electrodes. Glycosylated PcCDH was found to have a 30% bigger hydrodynamic radius than dPcCDH using dynamic light scattering. The basic bioelectrochemistry as well as the bioelectrocatalytic properties are presented. (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
Analytical Chemistry
volume
84
issue
23
pages
10315 - 10323
publisher
The American Chemical Society
external identifiers
  • wos:000311815300025
  • scopus:84870499516
ISSN
1520-6882
DOI
10.1021/ac3022899
language
English
LU publication?
yes
id
8444e2cc-23e5-487f-b96a-aca7d2c4b563 (old id 3366184)
date added to LUP
2013-01-23 11:18:37
date last changed
2017-09-24 03:11:12
@article{8444e2cc-23e5-487f-b96a-aca7d2c4b563,
  abstract     = {Cellobiose dehydrogenase (CDH) is a monomeric extracellular flavocytochrome composed of a catalytic dehydrogenase domain (DHCDH) containing flavin adenine dinucleotide (FAD), a cytochrome domain (CYTCDH) containing heme b, and a linker region connecting the two domains. In this work, the effect of deglycosylation on the electrochemical properties of CDH from Phanerochaete chrysosporium (PcCDH) and Ceriporiopsis subvermispora (CsCDH) is presented. All the glycosylated and deglycosylated enzymes show direct electron transfer (DET) between the CYTCDH and the electrode. Graphite electrodes modified with deglycosylated PcCDH (dPcCDH) and CsCDH (dCsCDH) have a 40-65% higher I-max value in the presence of substrate than electrodes modified with their glycosylated counterparts. CsCDH trapped under a permselective membrane showed similar changes on gold electrodes protected by a thiol-based self-assembled monolayer (SAM), in contrast to PcCDH for which deglycosylation did not exhibit any different electrocatalytical response on SAM-modified gold electrodes. Glycosylated PcCDH was found to have a 30% bigger hydrodynamic radius than dPcCDH using dynamic light scattering. The basic bioelectrochemistry as well as the bioelectrocatalytic properties are presented.},
  author       = {Ortiz, Roberto and Matsumura, Hirotoshi and Tasca, Federico and Zahma, Kawah and Samejima, Masahiro and Igarashi, Kiyohiko and Ludwig, Roland and Gorton, Lo},
  issn         = {1520-6882},
  language     = {eng},
  number       = {23},
  pages        = {10315--10323},
  publisher    = {The American Chemical Society},
  series       = {Analytical Chemistry},
  title        = {Effect of Deglycosylation of Cellobiose Dehydrogenases on the Enhancement of Direct Electron Transfer with Electrodes},
  url          = {http://dx.doi.org/10.1021/ac3022899},
  volume       = {84},
  year         = {2012},
}