TY  - JOUR
A1  - Badalyan, Artavazd
A1  - Yoga, Etienne Galemou
A1  - Schwuchow, Viola
A1  - Pöller, Sascha
A1  - Schuhmann, Wolfgang
A1  - Leimkühler, Silke
A1  - Wollenberger, Ursula
T1  - Analysis of the interaction of the molybdenum hydroxylase PaoABC from Escherichia coli with positively and negatively charged metal complexes
JF  - Electrochemistry communications : an international journal dedicated to rapid publications in electrochemistry
N2  - An unusual behavior of the periplasmic aldehyde oxidoreductase (PaoABC) from Escherichia coil has been observed from electrochemical investigations of the enzyme catalyzed oxidation of aromatic aldehydes with different mediators under different conditions of ionic strength. The enzyme has similarity to other molybdoenzymes of the xanthine oxidase family, but the catalytic behavior turned out to be very different. Under steady state conditions the turnover of PaoABC is maximal at pH 4 for the negatively charged ferricyanide and at pH 9 for a positively charged osmium complex. Stopped-flow kinetic measurements of the catalytic half reaction showed that oxidation of benzaldehyde proceeds also above pH 7. Thus, benzaldehyde oxidation can proceed under acidic and basic conditions using this enzyme, a property which has not been described before for molybdenum hydroxylases. It is also suggested that the electron transfer with artificial electron acceptors and PaoABC can proceed at different protein sites and depends on the nature of the electron acceptor in addition to the ionic strength. (C) 2013 Elsevier B.V. All rights reserved.
KW  - Electron transfer
KW  - Multi-cofactor enzymes
KW  - Molybdoenzymes
KW  - Aldehyde oxidoreductase
Y1  - 2013
U6  - https://doi.org/10.1016/j.elecom.2013.09.017
SN  - 1388-2481
SN  - 1873-1902
VL  - 37
SP  - 5
EP  - 7
PB  - Elsevier
CY  - New York
ER  - 
TY  - JOUR
A1  - Han, Xiao Xia
A1  - Li, Junbo
A1  - Öner, Ibrahim Halil
A1  - Zhao, Bing
A1  - Leimkühler, Silke
A1  - Hildebrandt, Peter
A1  - Weidinger, Inez M.
T1  - Nickel electrodes as a cheap and versatile platform for studying structure and function of immobilized redox proteins
JF  - Analytica chimica acta : an international journal devoted to all branches of analytical chemistry
N2  - Practical use of many bioelectronic and bioanalytical devices is limited by the need of expensive materials and time consuming fabrication. Here we demonstrate the use of nickel electrodes as a simple and cheap solid support material for bioelectronic applications. The naturally nanostructured electrodes showed a surprisingly high electromagnetic surface enhancement upon light illumination such that immobilization and electron transfer reactions of the model redox proteins cytochrome b(5) (Cyt b(5)) and cytochrome c (Cyt c) could be followed via surface enhanced resonance Raman spectroscopy. It could be shown that the nickel surface, when used as received, promotes a very efficient binding of the proteins upon preservation of their native structure. The immobilized redox proteins could efficiently exchange electrons with the electrode and could even act as an electron relay between the electrode and solubilized myoglobin. Our results open up new possibility for nickel electrodes as an exceptional good support for bioelectronic devices and biosensors on the one hand and for surface enhanced spectroscopic investigations on the other hand. (C) 2016 Elsevier B.V. All rights reserved.
KW  - Ni electrodes
KW  - Redox proteins
KW  - Surface enhanced Raman spectroscopy
KW  - Electron relay
KW  - Biocompatibility
KW  - Electron transfer
Y1  - 2016
U6  - https://doi.org/10.1016/j.aca.2016.08.053
SN  - 0003-2670
SN  - 1873-4324
VL  - 941
SP  - 35
EP  - 40
PB  - Elsevier
CY  - Amsterdam
ER  - 
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  -