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|dc.identifier.citation||Biochemical and Biophysical Research Communications, 2007; 360(3):666-672||en|
|dc.description.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.||en|
|dc.description.statementofresponsibility||Stephen G. Bell, Luet-Lok Wong||en|
|dc.publisher||Academic Press Inc||en|
|dc.rights||© 2007 Elsevier Inc. All rights reserved.||en|
|dc.subject||Novosphingobium aromaticivorans; P450 enzymes; Substrate specificity; Monooxygenases; Electron transfer||en|
|dc.title||P450 enzymes from the bacterium Novosphingobium aromaticivorans||en|
|pubs.library.collection||Chemistry and Physics publications||en|
|dc.identifier.orcid||Bell, S. [0000-0002-7457-9727]||en|
|Appears in Collections:||Chemistry and Physics publications|
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