TY  - JOUR
A1  - Pinyou, Piyanut
A1  - Ruff, Adrian
A1  - Poeller, Sascha
A1  - Alsaoub, Sabine
A1  - Leimkühler, Silke
A1  - Wollenberger, Ursula
A1  - Schuhmann, Wolfgang
T1  - Wiring of the aldehyde oxidoreductase PaoABC to electrode surfaces via entrapment in low potential phenothiazine-modified redox polymers
JF  - Bioelectrochemistry : an international journal devoted to electrochemical aspects of biology and biological aspects of electrochemistry ; official journal of the Bioelectrochemical Society
N2  - Phenothiazine-modified redox hydrogels were synthesized and used for the wiring of the aldehyde oxidoreductase PaoABC to electrode surfaces. The effects of the pH value and electrode surface modification on the biocatalytic activity of the layers were studied in the presence of vanillin as the substrate. The enzyme electrodes were successfully employed as bioanodes in vanillin/O-2 biofuel cells in combination with a high potential bilirubin oxidase biocathode. Open circuit voltages of around 700 mV could be obtained in a two compartment biofuel cell setup. Moreover, the use of a rather hydrophobic polymer with a high degree of crosslinking sites ensures the formation of stable polymer/enzyme films which were successfully used as bioanode in membrane-less biofuel cells. (C) 2015 Elsevier B.V. All rights reserved.
KW  - Aldehyde oxidoreductase
KW  - Enzyme electrode
KW  - Redox polymer
KW  - Phenothiazine
KW  - Biosensor
KW  - Biofuel cell
Y1  - 2016
U6  - https://doi.org/10.1016/j.bioelechem.2015.12.005
SN  - 1567-5394
SN  - 1878-562X
VL  - 109
SP  - 24
EP  - 30
PB  - Elsevier
CY  - Lausanne
ER  - 
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  -