Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications.
(2010) In ChemPhysChem 11. p.2674-2697- Abstract
- Cellobiose dehydrogenase catalyses the oxidation of aldoses-a simple reaction, a boring enzyme? No, neither for the envisaged bioelectrochemical applications nor mechanistically. The catalytic cycle of this flavocytochrome is complex and modulated by its flexible cytochrome domain, which acts as a built-in redox mediator. This intramolecular electron transfer is modulated by the pH, an adaptation to the environmental conditions encountered or created by the enzyme-producing fungi. The cytochrome domain forms the base from which electrons can jump to large terminal electron acceptors, such as redox proteins, and also enables by that path direct electron transfer from the catalytically active flavodehydrogenase domain to electrode surfaces.... (More)
- Cellobiose dehydrogenase catalyses the oxidation of aldoses-a simple reaction, a boring enzyme? No, neither for the envisaged bioelectrochemical applications nor mechanistically. The catalytic cycle of this flavocytochrome is complex and modulated by its flexible cytochrome domain, which acts as a built-in redox mediator. This intramolecular electron transfer is modulated by the pH, an adaptation to the environmental conditions encountered or created by the enzyme-producing fungi. The cytochrome domain forms the base from which electrons can jump to large terminal electron acceptors, such as redox proteins, and also enables by that path direct electron transfer from the catalytically active flavodehydrogenase domain to electrode surfaces. The application of electrochemical techniques to the elucidation of the molecular and catalytic properties of cellobiose dehydrogenase is discussed and compared to biochemical methods. The results lead to valuable insights into the function of this cellulose-bound enzyme, but also form the basis of exciting applications in biosensors, biofuel cells and bioelectrocatalysis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1644525
- author
- Ludwig, Roland ; Harreither, Wolfgang LU ; Tasca, Federico LU and Gorton, Lo LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- ChemPhysChem
- volume
- 11
- pages
- 2674 - 2697
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000282539100002
- pmid:20661990
- scopus:77956791837
- pmid:20661990
- ISSN
- 1439-7641
- DOI
- 10.1002/cphc.201000216
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004), Biochemistry and Structural Biology (S) (000006142)
- id
- fa98aee5-1981-4b48-8aae-d195cc985b65 (old id 1644525)
- date added to LUP
- 2016-04-01 10:56:25
- date last changed
- 2023-11-10 08:55:04
@article{fa98aee5-1981-4b48-8aae-d195cc985b65,
abstract = {{Cellobiose dehydrogenase catalyses the oxidation of aldoses-a simple reaction, a boring enzyme? No, neither for the envisaged bioelectrochemical applications nor mechanistically. The catalytic cycle of this flavocytochrome is complex and modulated by its flexible cytochrome domain, which acts as a built-in redox mediator. This intramolecular electron transfer is modulated by the pH, an adaptation to the environmental conditions encountered or created by the enzyme-producing fungi. The cytochrome domain forms the base from which electrons can jump to large terminal electron acceptors, such as redox proteins, and also enables by that path direct electron transfer from the catalytically active flavodehydrogenase domain to electrode surfaces. The application of electrochemical techniques to the elucidation of the molecular and catalytic properties of cellobiose dehydrogenase is discussed and compared to biochemical methods. The results lead to valuable insights into the function of this cellulose-bound enzyme, but also form the basis of exciting applications in biosensors, biofuel cells and bioelectrocatalysis.}},
author = {{Ludwig, Roland and Harreither, Wolfgang and Tasca, Federico and Gorton, Lo}},
issn = {{1439-7641}},
language = {{eng}},
pages = {{2674--2697}},
publisher = {{John Wiley & Sons Inc.}},
series = {{ChemPhysChem}},
title = {{Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications.}},
url = {{http://dx.doi.org/10.1002/cphc.201000216}},
doi = {{10.1002/cphc.201000216}},
volume = {{11}},
year = {{2010}},
}