Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris
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 {approx}2.0 A have been obtained.
- Authors:
-
- 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)
- Publication Date:
- OSTI Identifier:
- 20798871
- Resource Type:
- Journal Article
- Journal Name:
- Biochemical and Biophysical Research Communications
- Additional Journal Information:
- Journal Volume: 342; Journal 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); Journal ID: ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 60 APPLIED LIFE SCIENCES; BENZALDEHYDE; BENZENE; BENZOIC ACID; CRYSTALS; ELECTRON TRANSFER; ENZYMES; FERREDOXIN; PHENOLS; PSEUDOMONAS; RHODOPSEUDOMONAS; SPECIFICITY; SUBSTRATES
Citation Formats
Bell, Stephen G, Hoskins, Nicola, Feng, Xu, Caprotti, Domenico, Zihe, Rao, and Wong, L -L. Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris. United States: N. p., 2006.
Web. doi:10.1016/j.bbrc.2006.01.133.
Bell, Stephen G, Hoskins, Nicola, Feng, Xu, Caprotti, Domenico, Zihe, Rao, & Wong, L -L. Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris. United States. https://doi.org/10.1016/j.bbrc.2006.01.133
Bell, Stephen G, Hoskins, Nicola, Feng, Xu, Caprotti, Domenico, Zihe, Rao, and Wong, L -L. 2006.
"Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris". United States. https://doi.org/10.1016/j.bbrc.2006.01.133.
@article{osti_20798871,
title = {Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris},
author = {Bell, Stephen G and Hoskins, Nicola and Feng, Xu and Caprotti, Domenico and Zihe, Rao and Wong, L -L},
abstractNote = {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.},
doi = {10.1016/j.bbrc.2006.01.133},
url = {https://www.osti.gov/biblio/20798871},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 1,
volume = 342,
place = {United States},
year = {Fri Mar 31 00:00:00 EST 2006},
month = {Fri Mar 31 00:00:00 EST 2006}
}