TY  - JOUR
A1  - Cazelles, R.
A1  - Lalaoui, N.
A1  - Hartmann, Tobias
A1  - Leimkühler, Silke
A1  - Wollenberger, Ursula
A1  - Antonietti, Markus
A1  - Cosnier, S.
T1  - Ready to use bioinformatics analysis as a tool to predict immobilisation strategies for protein direct electron transfer (DET)
JF  - Polymer : the international journal for the science and technology of polymers
KW  - Bioinformatic
KW  - Bioelectrocatalysis
KW  - Electron transfer
KW  - Dehydrogenase
KW  - Nicotinamide
Y1  - 2016
U6  - https://doi.org/10.1016/j.bios.2016.04.078
SN  - 0956-5663
SN  - 1873-4235
VL  - 85
SP  - 90
EP  - 95
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Frasca, Stefano
A1  - Milan, Anabel Molero
A1  - Guiet, Amandine
A1  - Goebel, Caren
A1  - Perez-Caballero, Fernando
A1  - Stiba, Konstanze
A1  - Leimkühler, Silke
A1  - Fischer, Anna
A1  - Wollenberger, Ursula
T1  - Bioelectrocatalysis at mesoporous antimony doped tin oxide
 electrodes-Electrochemical characterization and direct enzyme
 communication
JF  - ELECTROCHIMICA ACTA
N2  - In this paper we report immobilization and bioelectrocatalysis of human sulfite oxidase (hSO) on nanostructured antimony doped tin oxide (ATO) thin film electrodes. Two types of ATO thin film electrodes were prepared via evaporation induced self-assembly of ATO nanoparticle sols. The use of a porogen results in different porosity and film thickness. Nevertheless both electrode types reveal similar quasi reversible electrochemical behavior for positive and negatively charged small mediators. Facile and durable immobilization of catalytically active enzyme in a direct electron transfer configuration was achieved without further chemical modification of the ATO surfaces. Interestingly, the binding of hSO onto the ATO surface seems to be not only of electrostatic nature, but also originates from a strong interaction between the histidine-tag of the enzyme and the supporting material. This is suggested from stable sulfite dependent bioelectrocatalytic signals at high ionic strength and imidazole desorption experiments. As such, ATO appears as a promising conductive platform for the immobilization of complex enzymes and their application in bioelectrocatalysis. (C) 2013 Elsevier Ltd. All rights reserved.
KW  - Antimony doped tin dioxide
KW  - Sulfite oxidase
KW  - Direct electrochemistry
KW  - Biosensor
KW  - Bioelectrocatalysis
Y1  - 2013
U6  - https://doi.org/10.1016/j.electacta.2013.03.144
SN  - 0013-4686
SN  - 1873-3859
VL  - 110
IS  - 2
SP  - 172
EP  - 180
PB  - PERGAMON-ELSEVIER SCIENCE LTD
CY  - OXFORD
ER  - 
TY  - JOUR
A1  - Zeng, Ting
A1  - Frasca, Stefano
A1  - Rumschöttel, Jens
A1  - Koetz, Joachim
A1  - Leimkühler, Silke
A1  - Wollenberger, Ursula
T1  - Role of Conductive Nanoparticles in the Direct Unmediated Bioelectrocatalysis of Immobilized Sulfite Oxidase
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
KW  - Direct electron transfer
KW  - Protein voltammetry
KW  - Human sulfite oxidase
KW  - Bioelectrocatalysis
KW  - Nanoparticles
Y1  - 2016
U6  - https://doi.org/10.1002/elan.201600246
SN  - 1040-0397
SN  - 1521-4109
VL  - 28
SP  - 2303
EP  - 2310
PB  - Wiley-VCH
CY  - Weinheim
ER  -