Cytochrome P450-catalyzed O-dealkylation coupled with photochemical NADPH regeneration
Cytochrome P450 monooxygenases are multifunctional enzymes with potential applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Widespread application of cytochrome P450s, however, is encumbered by the critical need for redox equivalents i...
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| Veröffentlicht in: | Biotechnology and bioengineering 2013-02, Vol.110 (2), p.383-390 |
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| creator | Lee, Sahng Ha Kwon, Yong-Chan Kim, Dong-Myung Park, Chan Beum |
| description | Cytochrome P450 monooxygenases are multifunctional enzymes with potential applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Widespread application of cytochrome P450s, however, is encumbered by the critical need for redox equivalents in their catalytic function. To overcome this limitation, we studied visible light‐driven regeneration of NADPH for P450‐catalyzed O‐dealkylation reaction; we used eosin Y as a photosensitizing dye, triethanolamine as an electron donor, and [Cp*Rh(bpy)H2O] as an electron mediator. We analyzed catalytic activity of cell‐free synthesized P450 BM3 monooxygenase variant (Y51F/F87A, BM3m2) in the presence of key components for NADPH photoregeneration. The P450‐catalyzed O‐dealkylation reaction sustainably maintained its turnover with the continuous supply of photoregenerated NADPH. Visible light‐driven, non‐enzymatic NADPH regeneration provides a new route for efficient, sustainable utilization of P450 monooxygenases. Biotechnol. Bioeng. 2013; 110: 383–390. © 2012 Wiley Periodicals, Inc.
Cytochrome P450 monooxygenases are multi‐functional enzymes with widespread applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Lee and coworkers performed a visible light‐driven photoenzymatic O‐dealkylation reaction by using a cell‐free synthesized P450 BM3 monooxygenase variant (BM3m2). A sustainable photoenzymatic reaction of the P450 BM3 was performed through visible light‐driven regeneration of NADPH from NADPH. The P450 biocatalysis, coupled with photochemical cofactor regeneration, suggests an excellent strategy for visible a light‐driven selective oxidation reaction. |
| doi_str_mv | 10.1002/bit.24729 |
| format | Article |
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Cytochrome P450 monooxygenases are multi‐functional enzymes with widespread applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Lee and coworkers performed a visible light‐driven photoenzymatic O‐dealkylation reaction by using a cell‐free synthesized P450 BM3 monooxygenase variant (BM3m2). A sustainable photoenzymatic reaction of the P450 BM3 was performed through visible light‐driven regeneration of NADPH from NADPH. The P450 biocatalysis, coupled with photochemical cofactor regeneration, suggests an excellent strategy for visible a light‐driven selective oxidation reaction.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.24729</identifier><identifier>PMID: 23007262</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Biotechnology - methods ; cell-free protein synthesis ; Cell-Free System ; Cells ; Chemicals ; cofactor regeneration ; Cytochrome P-450 Enzyme System - metabolism ; cytochrome P450 ; Dealkylation ; Electrons ; Enzymes ; Eosine Yellowish-(YS) - chemistry ; Light ; Metabolic Networks and Pathways ; Metabolism ; NADP - analysis ; NADP - metabolism ; NADPH ; Oxidation-Reduction ; Photobioreactors ; Photochemical Processes ; photosynthesis ; redox enzymes</subject><ispartof>Biotechnology and bioengineering, 2013-02, Vol.110 (2), p.383-390</ispartof><rights>Copyright © 2012 Wiley Periodicals, Inc.</rights><rights>Copyright John Wiley and Sons, Limited Feb 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4249-4354b339d757f12f16dbfa36c959eb24b8dfc9b24327b18f1973c301e3d06f423</citedby><cites>FETCH-LOGICAL-c4249-4354b339d757f12f16dbfa36c959eb24b8dfc9b24327b18f1973c301e3d06f423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbit.24729$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.24729$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23007262$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Sahng Ha</creatorcontrib><creatorcontrib>Kwon, Yong-Chan</creatorcontrib><creatorcontrib>Kim, Dong-Myung</creatorcontrib><creatorcontrib>Park, Chan Beum</creatorcontrib><title>Cytochrome P450-catalyzed O-dealkylation coupled with photochemical NADPH regeneration</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>Cytochrome P450 monooxygenases are multifunctional enzymes with potential applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Widespread application of cytochrome P450s, however, is encumbered by the critical need for redox equivalents in their catalytic function. To overcome this limitation, we studied visible light‐driven regeneration of NADPH for P450‐catalyzed O‐dealkylation reaction; we used eosin Y as a photosensitizing dye, triethanolamine as an electron donor, and [Cp*Rh(bpy)H2O] as an electron mediator. We analyzed catalytic activity of cell‐free synthesized P450 BM3 monooxygenase variant (Y51F/F87A, BM3m2) in the presence of key components for NADPH photoregeneration. The P450‐catalyzed O‐dealkylation reaction sustainably maintained its turnover with the continuous supply of photoregenerated NADPH. Visible light‐driven, non‐enzymatic NADPH regeneration provides a new route for efficient, sustainable utilization of P450 monooxygenases. Biotechnol. Bioeng. 2013; 110: 383–390. © 2012 Wiley Periodicals, Inc.
Cytochrome P450 monooxygenases are multi‐functional enzymes with widespread applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Lee and coworkers performed a visible light‐driven photoenzymatic O‐dealkylation reaction by using a cell‐free synthesized P450 BM3 monooxygenase variant (BM3m2). A sustainable photoenzymatic reaction of the P450 BM3 was performed through visible light‐driven regeneration of NADPH from NADPH. The P450 biocatalysis, coupled with photochemical cofactor regeneration, suggests an excellent strategy for visible a light‐driven selective oxidation reaction.</description><subject>Biotechnology - methods</subject><subject>cell-free protein synthesis</subject><subject>Cell-Free System</subject><subject>Cells</subject><subject>Chemicals</subject><subject>cofactor regeneration</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>cytochrome P450</subject><subject>Dealkylation</subject><subject>Electrons</subject><subject>Enzymes</subject><subject>Eosine Yellowish-(YS) - chemistry</subject><subject>Light</subject><subject>Metabolic Networks and Pathways</subject><subject>Metabolism</subject><subject>NADP - analysis</subject><subject>NADP - metabolism</subject><subject>NADPH</subject><subject>Oxidation-Reduction</subject><subject>Photobioreactors</subject><subject>Photochemical Processes</subject><subject>photosynthesis</subject><subject>redox enzymes</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U1PFTEUBuDGSOSCLvwDZhI3shg4_Z4u4SpfQSARcdl0Oh3vQOf22s4Exl9v4QILE-Oqp81z3qR5EXqPYRcDkL26G3YJk0S9QjMMSpZAFLxGMwAQJeWKbKKtlG7yVVZCvEGbhOaRCDJD1_NpCHYRQ--KS8ahtGYwfvrtmuKibJzxt5M3QxeWhQ3jyufnu25YFKtFeFhzfWeNL873P18eF9H9dEsXH_VbtNEan9y7p3MbfT_8cjU_Ls8ujk7m-2elZYSpklHOakpVI7lsMWmxaOrWUGEVV64mrK6a1qo8UCJrXLVYSWopYEcbEC0jdBt9WueuYvg1ujTovkvWeW-WLoxJY0YZEF5J_H9KJMVYUJCZfvyL3oQxLvNHsuKYUw5KZbWzVjaGlKJr9Sp2vYmTxqAfetG5F_3YS7YfnhLHunfNi3wuIoO9NbjrvJv-naQPTq6eI8v1RpcGd_-yYeKtFpJKrn-cH-nTr9cM8DfQFf0D2HOjiA</recordid><startdate>201302</startdate><enddate>201302</enddate><creator>Lee, Sahng Ha</creator><creator>Kwon, Yong-Chan</creator><creator>Kim, Dong-Myung</creator><creator>Park, Chan Beum</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>201302</creationdate><title>Cytochrome P450-catalyzed O-dealkylation coupled with photochemical NADPH regeneration</title><author>Lee, Sahng Ha ; Kwon, Yong-Chan ; Kim, Dong-Myung ; Park, Chan Beum</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4249-4354b339d757f12f16dbfa36c959eb24b8dfc9b24327b18f1973c301e3d06f423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Biotechnology - methods</topic><topic>cell-free protein synthesis</topic><topic>Cell-Free System</topic><topic>Cells</topic><topic>Chemicals</topic><topic>cofactor regeneration</topic><topic>Cytochrome P-450 Enzyme System - metabolism</topic><topic>cytochrome P450</topic><topic>Dealkylation</topic><topic>Electrons</topic><topic>Enzymes</topic><topic>Eosine Yellowish-(YS) - chemistry</topic><topic>Light</topic><topic>Metabolic Networks and Pathways</topic><topic>Metabolism</topic><topic>NADP - analysis</topic><topic>NADP - metabolism</topic><topic>NADPH</topic><topic>Oxidation-Reduction</topic><topic>Photobioreactors</topic><topic>Photochemical Processes</topic><topic>photosynthesis</topic><topic>redox enzymes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Sahng Ha</creatorcontrib><creatorcontrib>Kwon, Yong-Chan</creatorcontrib><creatorcontrib>Kim, Dong-Myung</creatorcontrib><creatorcontrib>Park, Chan Beum</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Sahng Ha</au><au>Kwon, Yong-Chan</au><au>Kim, Dong-Myung</au><au>Park, Chan Beum</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochrome P450-catalyzed O-dealkylation coupled with photochemical NADPH regeneration</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>2013-02</date><risdate>2013</risdate><volume>110</volume><issue>2</issue><spage>383</spage><epage>390</epage><pages>383-390</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><coden>BIBIAU</coden><abstract>Cytochrome P450 monooxygenases are multifunctional enzymes with potential applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Widespread application of cytochrome P450s, however, is encumbered by the critical need for redox equivalents in their catalytic function. To overcome this limitation, we studied visible light‐driven regeneration of NADPH for P450‐catalyzed O‐dealkylation reaction; we used eosin Y as a photosensitizing dye, triethanolamine as an electron donor, and [Cp*Rh(bpy)H2O] as an electron mediator. We analyzed catalytic activity of cell‐free synthesized P450 BM3 monooxygenase variant (Y51F/F87A, BM3m2) in the presence of key components for NADPH photoregeneration. The P450‐catalyzed O‐dealkylation reaction sustainably maintained its turnover with the continuous supply of photoregenerated NADPH. Visible light‐driven, non‐enzymatic NADPH regeneration provides a new route for efficient, sustainable utilization of P450 monooxygenases. Biotechnol. Bioeng. 2013; 110: 383–390. © 2012 Wiley Periodicals, Inc.
Cytochrome P450 monooxygenases are multi‐functional enzymes with widespread applications in chemoenzymatic synthesis of complex chemicals as well as in studies of metabolism and xenobiotics. Lee and coworkers performed a visible light‐driven photoenzymatic O‐dealkylation reaction by using a cell‐free synthesized P450 BM3 monooxygenase variant (BM3m2). A sustainable photoenzymatic reaction of the P450 BM3 was performed through visible light‐driven regeneration of NADPH from NADPH. The P450 biocatalysis, coupled with photochemical cofactor regeneration, suggests an excellent strategy for visible a light‐driven selective oxidation reaction.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>23007262</pmid><doi>10.1002/bit.24729</doi><tpages>8</tpages></addata></record> |
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| subjects | Biotechnology - methods cell-free protein synthesis Cell-Free System Cells Chemicals cofactor regeneration Cytochrome P-450 Enzyme System - metabolism cytochrome P450 Dealkylation Electrons Enzymes Eosine Yellowish-(YS) - chemistry Light Metabolic Networks and Pathways Metabolism NADP - analysis NADP - metabolism NADPH Oxidation-Reduction Photobioreactors Photochemical Processes photosynthesis redox enzymes |
| title | Cytochrome P450-catalyzed O-dealkylation coupled with photochemical NADPH regeneration |
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