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Investigation of electron transfer between cellobiose dehydrogenase from Myriococcum Thermophilum and gold electrodes

Coman, Vasile LU ; Harreither, Wolfgang; Ludwig, Roland; Haltrich, Dietmar and Gorton, Lo (2007) In Chemical Analysis 52(6). p.945-960
Abstract
Cellobiose dehydrogenase (CDH) is a monomeric protein consisting of two subdomains: a larger flavin-associated domain (DHcdh) and a smaller heme-binding domain (CYTcdh), connected via a protease cleavable linker region. In this study, the inter-domain electron transfer, using the CDH from the ascomycete fungus Myriococcum thermophilum and thiol (SAM) modified gold electrodes, was investigated with cyclic voltammetry and UV-VIS spectroelectrochemistry. The effect of the SAM and pH on the formal potential of the heme domain of CDH and on the current generated by the electrocatalytic oxidation of cellobiose and lactose was evaluated with voltammetric techniques. The oxidation-reduction midpoint potentials of the DHcdh, CYTcdh, and whole CDH... (More)
Cellobiose dehydrogenase (CDH) is a monomeric protein consisting of two subdomains: a larger flavin-associated domain (DHcdh) and a smaller heme-binding domain (CYTcdh), connected via a protease cleavable linker region. In this study, the inter-domain electron transfer, using the CDH from the ascomycete fungus Myriococcum thermophilum and thiol (SAM) modified gold electrodes, was investigated with cyclic voltammetry and UV-VIS spectroelectrochemistry. The effect of the SAM and pH on the formal potential of the heme domain of CDH and on the current generated by the electrocatalytic oxidation of cellobiose and lactose was evaluated with voltammetric techniques. The oxidation-reduction midpoint potentials of the DHcdh, CYTcdh, and whole CDH unit were estimated at different pH values using a long-optical-pathway thin capillary-type spectroelectrochemical cell. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
electrode, thiol modified gold, cellobiose dehydrogenase, Myriococcum thermophilum, direct electron transfer, bioelectrocatalysis
in
Chemical Analysis
volume
52
issue
6
pages
945 - 960
publisher
Polskie Towarzystwo Chemiczne - Polish Chemical Society
external identifiers
  • wos:000252951200007
  • scopus:39649094088
ISSN
0009-2223
language
English
LU publication?
yes
id
c1b7558a-f7e0-4fb9-9d6c-f73fd9a6fa4c (old id 1407572)
date added to LUP
2009-06-02 10:18:10
date last changed
2017-09-24 04:34:00
@article{c1b7558a-f7e0-4fb9-9d6c-f73fd9a6fa4c,
  abstract     = {Cellobiose dehydrogenase (CDH) is a monomeric protein consisting of two subdomains: a larger flavin-associated domain (DHcdh) and a smaller heme-binding domain (CYTcdh), connected via a protease cleavable linker region. In this study, the inter-domain electron transfer, using the CDH from the ascomycete fungus Myriococcum thermophilum and thiol (SAM) modified gold electrodes, was investigated with cyclic voltammetry and UV-VIS spectroelectrochemistry. The effect of the SAM and pH on the formal potential of the heme domain of CDH and on the current generated by the electrocatalytic oxidation of cellobiose and lactose was evaluated with voltammetric techniques. The oxidation-reduction midpoint potentials of the DHcdh, CYTcdh, and whole CDH unit were estimated at different pH values using a long-optical-pathway thin capillary-type spectroelectrochemical cell.},
  author       = {Coman, Vasile and Harreither, Wolfgang and Ludwig, Roland and Haltrich, Dietmar and Gorton, Lo},
  issn         = {0009-2223},
  keyword      = {electrode,thiol modified gold,cellobiose dehydrogenase,Myriococcum thermophilum,direct electron transfer,bioelectrocatalysis},
  language     = {eng},
  number       = {6},
  pages        = {945--960},
  publisher    = {Polskie Towarzystwo Chemiczne - Polish Chemical Society},
  series       = {Chemical Analysis},
  title        = {Investigation of electron transfer between cellobiose dehydrogenase from Myriococcum Thermophilum and gold electrodes},
  volume       = {52},
  year         = {2007},
}