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  • Title: Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris.
    Author: Bell SG, Hoskins N, Xu F, Caprotti D, Rao Z, Wong LL.
    Journal: Biochem Biophys Res Commun; 2006 Mar 31; 342(1):191-6. PubMed ID: 16472768.
    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 approximately 2.0A have been obtained.
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