Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris
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, a...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-03, Vol.342 (1), p.191-196 |
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| creator | Bell, Stephen G. Hoskins, Nicola Xu, Feng Caprotti, Domenico Rao, Zihe Wong, Luet-Lok |
| description | 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 ∼2.0Å have been obtained. |
| doi_str_mv | 10.1016/j.bbrc.2006.01.133 |
| format | Article |
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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. 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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 ∼2.0Å have been obtained.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>BENZALDEHYDE</subject><subject>BENZENE</subject><subject>BENZOIC ACID</subject><subject>Catalysis</subject><subject>Crystallization</subject><subject>CRYSTALS</subject><subject>Cytochrome P-450 Enzyme System - chemistry</subject><subject>Cytochrome P-450 Enzyme System - genetics</subject><subject>Cytochrome P-450 Enzyme System - isolation & purification</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>ELECTRON TRANSFER</subject><subject>ENZYMES</subject><subject>FERREDOXIN</subject><subject>Gene Expression</subject><subject>Monooxygenases</subject><subject>P450 enzymes</subject><subject>PHENOLS</subject><subject>PSEUDOMONAS</subject><subject>Pseudomonas putida</subject><subject>RHODOPSEUDOMONAS</subject><subject>Rhodopseudomonas - classification</subject><subject>Rhodopseudomonas - enzymology</subject><subject>Rhodopseudomonas - genetics</subject><subject>Rhodopseudomonas - metabolism</subject><subject>Rhodopseudomonas palustris</subject><subject>SPECIFICITY</subject><subject>Spectrum Analysis</subject><subject>Substrate Specificity</subject><subject>SUBSTRATES</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkd-L1DAQx4Mo3nr6D_ggBcG31pk2TVLwRRZ_wcEdh4LgQ0iTWTZL26xJerD-9bbsgm_eUyD5zDcz82HsNUKFgOL9oer7aKsaQFSAFTbNE7ZB6KCsEfhTtoHlpaw7_HnFXqR0AEDkonvOrlBwWUuhNuzX9pSD3ccwUnHHWyho-nMaKRW75arIeypGyqYPg7dmGE6F8w8UExW9sZmin8fifh9cOCaaXRjDZFJxNMOccvTpJXu2M0OiV5fzmv34_On79mt5c_vl2_bjTWm57HIpXY1t2wipTCNbDtgCcVQ9gmh4t0OqOw5WNeBkg63lyijuLIGw6IQB3lyzt-fckLLXyfpMdm_DNJHNugbZKSVxod6dqWMMv2dKWY8-WRoGM1GYkxZSSOhE8yiIculM8fXf-gzaGFKKtNPH6EcTTxpBr4b0Qa-G9GpIA-rF0FL05pI-9yO5fyUXJQvw4QzQsrIHT3GdiCZLzsd1IBf8__L_ArJtoLU</recordid><startdate>20060331</startdate><enddate>20060331</enddate><creator>Bell, Stephen G.</creator><creator>Hoskins, Nicola</creator><creator>Xu, Feng</creator><creator>Caprotti, Domenico</creator><creator>Rao, Zihe</creator><creator>Wong, Luet-Lok</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20060331</creationdate><title>Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris</title><author>Bell, Stephen G. ; Hoskins, Nicola ; Xu, Feng ; Caprotti, Domenico ; Rao, Zihe ; Wong, Luet-Lok</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c479t-7d21553678a37540150e418b106349f1e2940c830d7315c48a84dce06c1d6a043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>BENZALDEHYDE</topic><topic>BENZENE</topic><topic>BENZOIC ACID</topic><topic>Catalysis</topic><topic>Crystallization</topic><topic>CRYSTALS</topic><topic>Cytochrome P-450 Enzyme System - chemistry</topic><topic>Cytochrome P-450 Enzyme System - genetics</topic><topic>Cytochrome P-450 Enzyme System - isolation & purification</topic><topic>Cytochrome P-450 Enzyme System - metabolism</topic><topic>ELECTRON TRANSFER</topic><topic>ENZYMES</topic><topic>FERREDOXIN</topic><topic>Gene Expression</topic><topic>Monooxygenases</topic><topic>P450 enzymes</topic><topic>PHENOLS</topic><topic>PSEUDOMONAS</topic><topic>Pseudomonas putida</topic><topic>RHODOPSEUDOMONAS</topic><topic>Rhodopseudomonas - classification</topic><topic>Rhodopseudomonas - enzymology</topic><topic>Rhodopseudomonas - genetics</topic><topic>Rhodopseudomonas - metabolism</topic><topic>Rhodopseudomonas palustris</topic><topic>SPECIFICITY</topic><topic>Spectrum Analysis</topic><topic>Substrate Specificity</topic><topic>SUBSTRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bell, Stephen G.</creatorcontrib><creatorcontrib>Hoskins, Nicola</creatorcontrib><creatorcontrib>Xu, Feng</creatorcontrib><creatorcontrib>Caprotti, Domenico</creatorcontrib><creatorcontrib>Rao, Zihe</creatorcontrib><creatorcontrib>Wong, Luet-Lok</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bell, Stephen G.</au><au>Hoskins, Nicola</au><au>Xu, Feng</au><au>Caprotti, Domenico</au><au>Rao, Zihe</au><au>Wong, Luet-Lok</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-03-31</date><risdate>2006</risdate><volume>342</volume><issue>1</issue><spage>191</spage><epage>196</epage><pages>191-196</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><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 ∼2.0Å have been obtained.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16472768</pmid><doi>10.1016/j.bbrc.2006.01.133</doi><tpages>6</tpages></addata></record> |
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| subjects | 60 APPLIED LIFE SCIENCES BENZALDEHYDE BENZENE BENZOIC ACID Catalysis Crystallization CRYSTALS Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - genetics Cytochrome P-450 Enzyme System - isolation & purification Cytochrome P-450 Enzyme System - metabolism ELECTRON TRANSFER ENZYMES FERREDOXIN Gene Expression Monooxygenases P450 enzymes PHENOLS PSEUDOMONAS Pseudomonas putida RHODOPSEUDOMONAS Rhodopseudomonas - classification Rhodopseudomonas - enzymology Rhodopseudomonas - genetics Rhodopseudomonas - metabolism Rhodopseudomonas palustris SPECIFICITY Spectrum Analysis Substrate Specificity SUBSTRATES |
| title | Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris |
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