Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris
- Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR (United Kingdom)
- Laboratory of Structural Biology, Department of Biological Science and Technology and MOE Laboratory of Protein Science, Tsinghua University, Beijing 100084 (China)
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 {approx}2.0 A have been obtained.
- OSTI ID:
- 20798871
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 342, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2006.01.133; PII: S0006-291X(06)00220-8; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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