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Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris
Authors:Bell Stephen G  Hoskins Nicola  Xu Feng  Caprotti Domenico  Rao Zihe  Wong Luet-Lok
Institution:Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK. stephen.bell@chem.ox.ac.uk
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.
Keywords:Rhodopseudomonas palustris  P450 enzymes  Substrate specificity  Monooxygenases  Electron transfer
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