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https://hdl.handle.net/2440/75784
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Type: | Journal article |
Title: | P450 enzymes from the bacterium Novosphingobium aromaticivorans |
Author: | Bell, S. Wong, L. |
Citation: | Biochemical and Biophysical Research Communications, 2007; 360(3):666-672 |
Publisher: | Academic Press Inc |
Issue Date: | 2007 |
ISSN: | 0006-291X 1090-2104 |
Statement of Responsibility: | Stephen G. Bell, Luet-Lok Wong |
Abstract: | Twelve of the fifteen potential P450 enzymes from the bacterium Novosphingobium aromaticivorans, which is known to degrade a wide range of aromatic hydrocarbons, have been produced via heterologous expression in Escherichia coli. The enzymes were tested for their ability to bind a range of substrates including polyaromatic hydrocarbons. While two of the enzymes were found to bind aromatic compounds (CYP108D1 and CYP203A2), the others show binding with a variety of compounds including linear alkanes (CYP153C1) and mono- and sesqui-terpenoid compounds (CYP101B1, CYP101C1, CYP101D1, CYP101D2, CYP111A1, and CYP219A1). A 2Fe–2S ferredoxin (Arx-A), which is associated with CYP101D2, was also produced. The activity of five of the P450 enzymes (CYP101B1, CYP101C1, CYP101D1, CYP101D2, and CYP111A2) was reconstituted with Arx-A and putidaredoxin reductase (of the P450cam system from Pseudomonas putida) in a Class I type electron transfer system. Preliminary characterisation of the majority of the substrate oxidation products is reported. |
Keywords: | Novosphingobium aromaticivorans P450 enzymes Substrate specificity Monooxygenases Electron transfer |
Rights: | © 2007 Elsevier Inc. All rights reserved. |
DOI: | 10.1016/j.bbrc.2007.06.119 |
Published version: | http://dx.doi.org/10.1016/j.bbrc.2007.06.119 |
Appears in Collections: | Aurora harvest Chemistry and Physics publications |
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