Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1940190 | Biochemical and Biophysical Research Communications | 2006 | 6 Pages |
Abstract
Four (CYP195A2, CYP199A2, CYP203A1, and CYP153A5) of the seven P450 enzymes, and palustrisredoxin A, a ferredoxin associated with CYP199A2, from the metabolically diverse bacterium Rhodopseudomonas palustris have been expressed and purified. A range of substituted benzenes, phenols, benzaldehydes, and benzoic acids was shown to bind to the four P450 enzymes. Monooxygenase activity of CYP199A2 was reconstituted with palustrisredoxin A and putidaredoxin reductase of the P450cam system from Pseudomonas putida. We found that 4-ethylbenzoate and 4-methoxybenzoate were oxidized to single products, and 4-methoxybenzoate was demethylated to form 4-hydroxybenzoate. Crystals of substrate-free CYP199A2 which diffracted to ∼2.0 Å have been obtained.
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Authors
Stephen G. Bell, Nicola Hoskins, Feng Xu, Domenico Caprotti, Zihe Rao, Luet-Lok Wong,