Cage Escape Competes with Geminate Recombination during Alkane Hydroxylation by the Diiron Oxygenase AlkB
AlkB stops the radical clock: Three structurally analogous radical‐clock substrates with a large span in their rearrangement rates are hydroxylated by AlkB to afford similar amounts of rearranged (2) and unrearranged products (1). Such a result is in accord with radical rebound competing with cage e...
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Veröffentlicht in: | Angewandte Chemie (International ed.) 2008-01, Vol.47 (28), p.5232-5234 |
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creator | Austin, Rachel N Luddy, Kate Erickson, Karla Pender-Cudlip, Marilla Bertrand, Erin Deng, Dayi Buzdygon, Ryan S van Beilen, Jan B Groves, John T |
description | AlkB stops the radical clock: Three structurally analogous radical‐clock substrates with a large span in their rearrangement rates are hydroxylated by AlkB to afford similar amounts of rearranged (2) and unrearranged products (1). Such a result is in accord with radical rebound competing with cage escape of the geminate substrate radical. The results show that radical clocks can measure both the radical lifetime and the kinetics of cage escape. |
doi_str_mv | 10.1002/anie.200801184 |
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Such a result is in accord with radical rebound competing with cage escape of the geminate substrate radical. The results show that radical clocks can measure both the radical lifetime and the kinetics of cage escape.</description><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.200801184</identifier><identifier>PMID: 18512839</identifier><language>eng</language><publisher>Weinheim: Wiley-VCH Verlag</publisher><subject>alkanes ; Alkanes - chemistry ; cytochrome AlkB ; Hydroxylation ; Kinetics ; Mixed Function Oxygenases - metabolism ; oxygenases ; Pseudomonas putida - enzymology ; radical clocks ; reaction mechanisms</subject><ispartof>Angewandte Chemie (International ed.), 2008-01, Vol.47 (28), p.5232-5234</ispartof><rights>Copyright © 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5004-96816c624b61547055d00ed42f962ec3f94e55c9e341673f6fc6a6963835411f3</citedby><cites>FETCH-LOGICAL-c5004-96816c624b61547055d00ed42f962ec3f94e55c9e341673f6fc6a6963835411f3</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%2Fanie.200801184$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fanie.200801184$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18512839$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Austin, Rachel N</creatorcontrib><creatorcontrib>Luddy, Kate</creatorcontrib><creatorcontrib>Erickson, Karla</creatorcontrib><creatorcontrib>Pender-Cudlip, Marilla</creatorcontrib><creatorcontrib>Bertrand, Erin</creatorcontrib><creatorcontrib>Deng, Dayi</creatorcontrib><creatorcontrib>Buzdygon, Ryan S</creatorcontrib><creatorcontrib>van Beilen, Jan B</creatorcontrib><creatorcontrib>Groves, John T</creatorcontrib><title>Cage Escape Competes with Geminate Recombination during Alkane Hydroxylation by the Diiron Oxygenase AlkB</title><title>Angewandte Chemie (International ed.)</title><addtitle>Angewandte Chemie International Edition</addtitle><description>AlkB stops the radical clock: Three structurally analogous radical‐clock substrates with a large span in their rearrangement rates are hydroxylated by AlkB to afford similar amounts of rearranged (2) and unrearranged products (1). Such a result is in accord with radical rebound competing with cage escape of the geminate substrate radical. The results show that radical clocks can measure both the radical lifetime and the kinetics of cage escape.</description><subject>alkanes</subject><subject>Alkanes - chemistry</subject><subject>cytochrome AlkB</subject><subject>Hydroxylation</subject><subject>Kinetics</subject><subject>Mixed Function Oxygenases - metabolism</subject><subject>oxygenases</subject><subject>Pseudomonas putida - enzymology</subject><subject>radical clocks</subject><subject>reaction mechanisms</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhiMEoqXlyhF84pbFjj8SX5C222VbUbVSP1SJi-V1JlnTJF7sLN38e7zKaiknTh7PPPOOPW-SfCB4QjDOvujOwiTDuMCEFOxVckx4RlKa5_R1jBmlaV5wcpS8C-Fn5IsCi7fJEYm5rKDyOLEzXQOaB6PXgGauXUMPAT3bfoUW0NpO94Buwbh2uYut61C58bar0bR50h2gi6H0bjs0Y205oH4F6NxaH28326GGTgfYwWenyZtKNwHe78-T5OHb_H52kV7dLC5n06vUcIxZKkVBhBEZWwrCWY45LzGGkmWVFBkYWkkGnBsJlBGR00pURmghBS0oZ4RU9CT5OuquN8sWSgNd73Wj1t622g_Kaav-rXR2pWr3W9E4n7A8CnzeC3j3awOhV60NBpom_tdtghIyi9uTMoKTETTeheChOgwhWO3cUTt31MGd2PDx5dP-4ns7IiBH4Nk2MPxHTk2vL-cvxdOx14Yetode7Z9U3FPO1eP1QuU_vp_LhXhUPPKfRr7STuna26Ae7jJMKMaSYF4I-gcPBrTr</recordid><startdate>20080101</startdate><enddate>20080101</enddate><creator>Austin, Rachel N</creator><creator>Luddy, Kate</creator><creator>Erickson, Karla</creator><creator>Pender-Cudlip, Marilla</creator><creator>Bertrand, Erin</creator><creator>Deng, Dayi</creator><creator>Buzdygon, Ryan S</creator><creator>van Beilen, Jan B</creator><creator>Groves, John T</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>FBQ</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080101</creationdate><title>Cage Escape Competes with Geminate Recombination during Alkane Hydroxylation by the Diiron Oxygenase AlkB</title><author>Austin, Rachel N ; Luddy, Kate ; Erickson, Karla ; Pender-Cudlip, Marilla ; Bertrand, Erin ; Deng, Dayi ; Buzdygon, Ryan S ; van Beilen, Jan B ; Groves, John T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5004-96816c624b61547055d00ed42f962ec3f94e55c9e341673f6fc6a6963835411f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>alkanes</topic><topic>Alkanes - chemistry</topic><topic>cytochrome AlkB</topic><topic>Hydroxylation</topic><topic>Kinetics</topic><topic>Mixed Function Oxygenases - metabolism</topic><topic>oxygenases</topic><topic>Pseudomonas putida - enzymology</topic><topic>radical clocks</topic><topic>reaction mechanisms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Austin, Rachel N</creatorcontrib><creatorcontrib>Luddy, Kate</creatorcontrib><creatorcontrib>Erickson, Karla</creatorcontrib><creatorcontrib>Pender-Cudlip, Marilla</creatorcontrib><creatorcontrib>Bertrand, Erin</creatorcontrib><creatorcontrib>Deng, Dayi</creatorcontrib><creatorcontrib>Buzdygon, Ryan S</creatorcontrib><creatorcontrib>van Beilen, Jan B</creatorcontrib><creatorcontrib>Groves, John T</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Angewandte Chemie (International ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Austin, Rachel N</au><au>Luddy, Kate</au><au>Erickson, Karla</au><au>Pender-Cudlip, Marilla</au><au>Bertrand, Erin</au><au>Deng, Dayi</au><au>Buzdygon, Ryan S</au><au>van Beilen, Jan B</au><au>Groves, John T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cage Escape Competes with Geminate Recombination during Alkane Hydroxylation by the Diiron Oxygenase AlkB</atitle><jtitle>Angewandte Chemie (International ed.)</jtitle><addtitle>Angewandte Chemie International Edition</addtitle><date>2008-01-01</date><risdate>2008</risdate><volume>47</volume><issue>28</issue><spage>5232</spage><epage>5234</epage><pages>5232-5234</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>AlkB stops the radical clock: Three structurally analogous radical‐clock substrates with a large span in their rearrangement rates are hydroxylated by AlkB to afford similar amounts of rearranged (2) and unrearranged products (1). Such a result is in accord with radical rebound competing with cage escape of the geminate substrate radical. The results show that radical clocks can measure both the radical lifetime and the kinetics of cage escape.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>18512839</pmid><doi>10.1002/anie.200801184</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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subjects | alkanes Alkanes - chemistry cytochrome AlkB Hydroxylation Kinetics Mixed Function Oxygenases - metabolism oxygenases Pseudomonas putida - enzymology radical clocks reaction mechanisms |
title | Cage Escape Competes with Geminate Recombination during Alkane Hydroxylation by the Diiron Oxygenase AlkB |
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