Analysis of the interaction of the molybdenum hydroxylase PaoABC from Escherichia coli with positively and negatively charged metal complexes
- 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 theAn 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.…
Verfasserangaben: | Artavazd BadalyanORCiDGND, Etienne Galemou Yoga, Viola Schwuchow, Sascha Pöller, Wolfgang Schuhmann, Silke LeimkühlerORCiDGND, Ursula WollenbergerORCiDGND |
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DOI: | https://doi.org/10.1016/j.elecom.2013.09.017 |
ISSN: | 1388-2481 |
ISSN: | 1873-1902 |
Titel des übergeordneten Werks (Englisch): | Electrochemistry communications : an international journal dedicated to rapid publications in electrochemistry |
Verlag: | Elsevier |
Verlagsort: | New York |
Publikationstyp: | Wissenschaftlicher Artikel |
Sprache: | Englisch |
Jahr der Erstveröffentlichung: | 2013 |
Erscheinungsjahr: | 2013 |
Datum der Freischaltung: | 26.03.2017 |
Freies Schlagwort / Tag: | Aldehyde oxidoreductase; Electron transfer; Molybdoenzymes; Multi-cofactor enzymes |
Band: | 37 |
Seitenanzahl: | 3 |
Erste Seite: | 5 |
Letzte Seite: | 7 |
Fördernde Institution: | Custer of Excellence "UniCat"; DFG [EXC 314]; Taschentuchlabor IZIB; BMBF [03IS2201B, 03IS2201F] |
Organisationseinheiten: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
Peer Review: | Referiert |