H 2 -driven biotransformation of n -octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O 2 -tolerant hydrogenase and a P450 monooxygenase
An in vivo biotransformation system is presented that affords the hydroxylation of n -octane to 1-octanol on the basis of NADH-dependent CYP153A monooxygenase and NAD + -reducing hydrogenase heterologously synthesized in a bacterial host. The hydrogenase sustains H 2 -driven NADH cofactor regenerati...
Gespeichert in:
Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2015-10, Vol.51 (90), p.16173-16175 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 16175 |
---|---|
container_issue | 90 |
container_start_page | 16173 |
container_title | Chemical communications (Cambridge, England) |
container_volume | 51 |
creator | Lonsdale, Thomas H. Lauterbach, Lars Honda Malca, Sumire Nestl, Bettina M. Hauer, Bernhard Lenz, Oliver |
description | An
in vivo
biotransformation system is presented that affords the hydroxylation of
n
-octane to 1-octanol on the basis of NADH-dependent CYP153A monooxygenase and NAD
+
-reducing hydrogenase heterologously synthesized in a bacterial host. The hydrogenase sustains H
2
-driven NADH cofactor regeneration even in the presence of O
2
, the co-substrate of monooxygenase. |
doi_str_mv | 10.1039/C5CC06078H |
format | Article |
fullrecord | <record><control><sourceid>crossref</sourceid><recordid>TN_cdi_crossref_primary_10_1039_C5CC06078H</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>10_1039_C5CC06078H</sourcerecordid><originalsourceid>FETCH-LOGICAL-c76H-9049ad120334c2513b9224591e9aad4ce92cc341850ba8d51445faadd14e34c63</originalsourceid><addsrcrecordid>eNpFkEFLAzEUhIMoWKsXf8E7C9Fkk2w3R1nUCkJ76MHbkk2ybaSblGQrrr_In2mWCr7LDAzzPRiEbim5p4TJh1rUNSnJolqeoRllJceCV-_nkxcSLxgXl-gqpQ-Sj4pqhn6WUAA20X1aD60LQ1Q-dSH2anDBQ-jAAw56UN7CEICefNhDO4KCaHXoW-eVH2Cd7NGEPniV4HAcnFGQMs150AGn0Q87m9y381tQHlbT1yHsbZyqu9HEsLW5aXNoMnjNBYHMCuFrPAXX6KJT-2Rv_nSONs9Pm3qJ31Yvr_XjG9aLcokl4VIZWhDGuC4EZa0sCi4ktVIpw7WVhdaM00qQVlVGUM5FlxNDuc2Nks3R3QmrY0gp2q45RNerODaUNNPEzf_E7BdbNHAV</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>H 2 -driven biotransformation of n -octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O 2 -tolerant hydrogenase and a P450 monooxygenase</title><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Lonsdale, Thomas H. ; Lauterbach, Lars ; Honda Malca, Sumire ; Nestl, Bettina M. ; Hauer, Bernhard ; Lenz, Oliver</creator><creatorcontrib>Lonsdale, Thomas H. ; Lauterbach, Lars ; Honda Malca, Sumire ; Nestl, Bettina M. ; Hauer, Bernhard ; Lenz, Oliver</creatorcontrib><description>An
in vivo
biotransformation system is presented that affords the hydroxylation of
n
-octane to 1-octanol on the basis of NADH-dependent CYP153A monooxygenase and NAD
+
-reducing hydrogenase heterologously synthesized in a bacterial host. The hydrogenase sustains H
2
-driven NADH cofactor regeneration even in the presence of O
2
, the co-substrate of monooxygenase.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/C5CC06078H</identifier><language>eng</language><ispartof>Chemical communications (Cambridge, England), 2015-10, Vol.51 (90), p.16173-16175</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c76H-9049ad120334c2513b9224591e9aad4ce92cc341850ba8d51445faadd14e34c63</citedby><cites>FETCH-LOGICAL-c76H-9049ad120334c2513b9224591e9aad4ce92cc341850ba8d51445faadd14e34c63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids></links><search><creatorcontrib>Lonsdale, Thomas H.</creatorcontrib><creatorcontrib>Lauterbach, Lars</creatorcontrib><creatorcontrib>Honda Malca, Sumire</creatorcontrib><creatorcontrib>Nestl, Bettina M.</creatorcontrib><creatorcontrib>Hauer, Bernhard</creatorcontrib><creatorcontrib>Lenz, Oliver</creatorcontrib><title>H 2 -driven biotransformation of n -octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O 2 -tolerant hydrogenase and a P450 monooxygenase</title><title>Chemical communications (Cambridge, England)</title><description>An
in vivo
biotransformation system is presented that affords the hydroxylation of
n
-octane to 1-octanol on the basis of NADH-dependent CYP153A monooxygenase and NAD
+
-reducing hydrogenase heterologously synthesized in a bacterial host. The hydrogenase sustains H
2
-driven NADH cofactor regeneration even in the presence of O
2
, the co-substrate of monooxygenase.</description><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNpFkEFLAzEUhIMoWKsXf8E7C9Fkk2w3R1nUCkJ76MHbkk2ybaSblGQrrr_In2mWCr7LDAzzPRiEbim5p4TJh1rUNSnJolqeoRllJceCV-_nkxcSLxgXl-gqpQ-Sj4pqhn6WUAA20X1aD60LQ1Q-dSH2anDBQ-jAAw56UN7CEICefNhDO4KCaHXoW-eVH2Cd7NGEPniV4HAcnFGQMs150AGn0Q87m9y381tQHlbT1yHsbZyqu9HEsLW5aXNoMnjNBYHMCuFrPAXX6KJT-2Rv_nSONs9Pm3qJ31Yvr_XjG9aLcokl4VIZWhDGuC4EZa0sCi4ktVIpw7WVhdaM00qQVlVGUM5FlxNDuc2Nks3R3QmrY0gp2q45RNerODaUNNPEzf_E7BdbNHAV</recordid><startdate>20151029</startdate><enddate>20151029</enddate><creator>Lonsdale, Thomas H.</creator><creator>Lauterbach, Lars</creator><creator>Honda Malca, Sumire</creator><creator>Nestl, Bettina M.</creator><creator>Hauer, Bernhard</creator><creator>Lenz, Oliver</creator><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20151029</creationdate><title>H 2 -driven biotransformation of n -octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O 2 -tolerant hydrogenase and a P450 monooxygenase</title><author>Lonsdale, Thomas H. ; Lauterbach, Lars ; Honda Malca, Sumire ; Nestl, Bettina M. ; Hauer, Bernhard ; Lenz, Oliver</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c76H-9049ad120334c2513b9224591e9aad4ce92cc341850ba8d51445faadd14e34c63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lonsdale, Thomas H.</creatorcontrib><creatorcontrib>Lauterbach, Lars</creatorcontrib><creatorcontrib>Honda Malca, Sumire</creatorcontrib><creatorcontrib>Nestl, Bettina M.</creatorcontrib><creatorcontrib>Hauer, Bernhard</creatorcontrib><creatorcontrib>Lenz, Oliver</creatorcontrib><collection>CrossRef</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lonsdale, Thomas H.</au><au>Lauterbach, Lars</au><au>Honda Malca, Sumire</au><au>Nestl, Bettina M.</au><au>Hauer, Bernhard</au><au>Lenz, Oliver</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>H 2 -driven biotransformation of n -octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O 2 -tolerant hydrogenase and a P450 monooxygenase</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><date>2015-10-29</date><risdate>2015</risdate><volume>51</volume><issue>90</issue><spage>16173</spage><epage>16175</epage><pages>16173-16175</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>An
in vivo
biotransformation system is presented that affords the hydroxylation of
n
-octane to 1-octanol on the basis of NADH-dependent CYP153A monooxygenase and NAD
+
-reducing hydrogenase heterologously synthesized in a bacterial host. The hydrogenase sustains H
2
-driven NADH cofactor regeneration even in the presence of O
2
, the co-substrate of monooxygenase.</abstract><doi>10.1039/C5CC06078H</doi><tpages>3</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1359-7345 |
ispartof | Chemical communications (Cambridge, England), 2015-10, Vol.51 (90), p.16173-16175 |
issn | 1359-7345 1364-548X |
language | eng |
recordid | cdi_crossref_primary_10_1039_C5CC06078H |
source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
title | H 2 -driven biotransformation of n -octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O 2 -tolerant hydrogenase and a P450 monooxygenase |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T15%3A00%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-crossref&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=H%202%20-driven%20biotransformation%20of%20n%20-octane%20to%201-octanol%20by%20a%20recombinant%20Pseudomonas%20putida%20strain%20co-synthesizing%20an%20O%202%20-tolerant%20hydrogenase%20and%20a%20P450%20monooxygenase&rft.jtitle=Chemical%20communications%20(Cambridge,%20England)&rft.au=Lonsdale,%20Thomas%20H.&rft.date=2015-10-29&rft.volume=51&rft.issue=90&rft.spage=16173&rft.epage=16175&rft.pages=16173-16175&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/C5CC06078H&rft_dat=%3Ccrossref%3E10_1039_C5CC06078H%3C/crossref%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |