Advanced

Catalytically Active Silica Nanoparticle-Based Supramolecular Architectures of Two Proteins - Cellobiose Dehydrogenase and Cytochrome c on Electrodes

Feifel, Sven C.; Ludwig, Roland; Gorton, Lo LU and Lisdat, Fred (2012) In Langmuir 28(25). p.9189-9194
Abstract
Artificial nanobiomolecular architectures that follow natural examples in protein assembly become more and more important from basic and applied points of view. Our study describes the investigation on cellobiose dehydrogenase (CDH), cytochrome c (cyt c), and silica nanoparticles (SiNP's) for the construction of fully catalytically active supramolecular architectures on electrodes. We report on intraprotein, interprotein, and direct electron-transfer reaction cascades of cellobiose dehydrogenase and cytochrome c immobilized in multiple supramolecular layers. Carboxy-modified SiNP's are used to provide an artificial matrix, which enables protein arrangement in an electroactive form. Direct and interprotein electron transfer has been... (More)
Artificial nanobiomolecular architectures that follow natural examples in protein assembly become more and more important from basic and applied points of view. Our study describes the investigation on cellobiose dehydrogenase (CDH), cytochrome c (cyt c), and silica nanoparticles (SiNP's) for the construction of fully catalytically active supramolecular architectures on electrodes. We report on intraprotein, interprotein, and direct electron-transfer reaction cascades of cellobiose dehydrogenase and cytochrome c immobilized in multiple supramolecular layers. Carboxy-modified SiNP's are used to provide an artificial matrix, which enables protein arrangement in an electroactive form. Direct and interprotein electron transfer has been established for a two-protein system with CDH and cyt c in a layered architecture for the first time. We also highlight that the glycosylation of CDH and the silica nanoparticle size play key roles in the mode of operation in such a complex system. The response of the specific substrate, here lactose, can be tuned by the number of immobilized nanobiomolecular layers. (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
25
pages
9189 - 9194
publisher
The American Chemical Society
external identifiers
  • wos:000305661400002
  • scopus:84862891001
ISSN
0743-7463
DOI
10.1021/la301290z
language
English
LU publication?
yes
id
eb72d6a2-e210-46ae-ae7b-87e17fe184a8 (old id 3001686)
date added to LUP
2012-08-21 11:02:38
date last changed
2017-11-19 03:07:22
@article{eb72d6a2-e210-46ae-ae7b-87e17fe184a8,
  abstract     = {Artificial nanobiomolecular architectures that follow natural examples in protein assembly become more and more important from basic and applied points of view. Our study describes the investigation on cellobiose dehydrogenase (CDH), cytochrome c (cyt c), and silica nanoparticles (SiNP's) for the construction of fully catalytically active supramolecular architectures on electrodes. We report on intraprotein, interprotein, and direct electron-transfer reaction cascades of cellobiose dehydrogenase and cytochrome c immobilized in multiple supramolecular layers. Carboxy-modified SiNP's are used to provide an artificial matrix, which enables protein arrangement in an electroactive form. Direct and interprotein electron transfer has been established for a two-protein system with CDH and cyt c in a layered architecture for the first time. We also highlight that the glycosylation of CDH and the silica nanoparticle size play key roles in the mode of operation in such a complex system. The response of the specific substrate, here lactose, can be tuned by the number of immobilized nanobiomolecular layers.},
  author       = {Feifel, Sven C. and Ludwig, Roland and Gorton, Lo and Lisdat, Fred},
  issn         = {0743-7463},
  language     = {eng},
  number       = {25},
  pages        = {9189--9194},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Catalytically Active Silica Nanoparticle-Based Supramolecular Architectures of Two Proteins - Cellobiose Dehydrogenase and Cytochrome c on Electrodes},
  url          = {http://dx.doi.org/10.1021/la301290z},
  volume       = {28},
  year         = {2012},
}