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  -