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Title: 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:
 [1];  [1];  [2];  [1];  [2];  [1]
  1. Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR (United Kingdom)
  2. 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}
}