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Article: A Substituted Hypersensitive Radical Probe for Enzyme-Catalyzed Hydroxylations: Synthesis of Racemic and Enantiomerically Enriched Forms and Application in a Cytochrome P450-Catalyzed Oxidation

TitleA Substituted Hypersensitive Radical Probe for Enzyme-Catalyzed Hydroxylations: Synthesis of Racemic and Enantiomerically Enriched Forms and Application in a Cytochrome P450-Catalyzed Oxidation
Authors
Issue Date1997
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/joc
Citation
Journal Of Organic Chemistry, 1997, v. 62 n. 26, p. 9114-9122 How to Cite?
AbstractThe syntheses of racemic and enantiomerically enriched trans-1-methyl-2-(4-(trifluoromethyl)phenyl)cyclopropane (3) and the possible oxidation products from enzyme-catalyzed hydroxylation of 3 at the methyl group are reported. The important intermediate in the production of 3 was the Weinreb amide of the 2-arylcyclopropanecarboxylic acid which could be prepared in diastereomerically pure form and which also served as an intermediate for production of the cyclic oxidation products of 3. Hydroxylation of 3 by the cytochrome P450 isozyme CYP2B1 gave cyclic and ring-opened products. The product ratios support an insertion mechanism for the enzyme-catalyzed hydroxylation reaction in which minor amounts of rearranged products are produced by radical fragmentation within the transition structure of the insertion and by a competing reaction involving a cationic species. Formation of cationic rearrangement products by a heterolytic fragmentation reaction of a first-formed protonated alcohol product is suggested on the basis of the apparent amounts of cationic products formed in the hydroxylation of 3. This pathway for cation production appears to require that the activated enzyme complex (equivalent to enzyme-substrate-H2O2) oxidizes substrate before water dissociates to give an iron-oxo species.
Persistent Identifierhttp://hdl.handle.net/10722/167275
ISSN
2015 Impact Factor: 4.785
2015 SCImago Journal Rankings: 2.095
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorToy, PHen_US
dc.contributor.authorDhanabalasingam, Ben_US
dc.contributor.authorNewcomb, Men_US
dc.contributor.authorHanna, IHen_US
dc.contributor.authorHollenberg, PFen_US
dc.date.accessioned2012-10-08T03:05:07Z-
dc.date.available2012-10-08T03:05:07Z-
dc.date.issued1997en_US
dc.identifier.citationJournal Of Organic Chemistry, 1997, v. 62 n. 26, p. 9114-9122en_US
dc.identifier.issn0022-3263en_US
dc.identifier.urihttp://hdl.handle.net/10722/167275-
dc.description.abstractThe syntheses of racemic and enantiomerically enriched trans-1-methyl-2-(4-(trifluoromethyl)phenyl)cyclopropane (3) and the possible oxidation products from enzyme-catalyzed hydroxylation of 3 at the methyl group are reported. The important intermediate in the production of 3 was the Weinreb amide of the 2-arylcyclopropanecarboxylic acid which could be prepared in diastereomerically pure form and which also served as an intermediate for production of the cyclic oxidation products of 3. Hydroxylation of 3 by the cytochrome P450 isozyme CYP2B1 gave cyclic and ring-opened products. The product ratios support an insertion mechanism for the enzyme-catalyzed hydroxylation reaction in which minor amounts of rearranged products are produced by radical fragmentation within the transition structure of the insertion and by a competing reaction involving a cationic species. Formation of cationic rearrangement products by a heterolytic fragmentation reaction of a first-formed protonated alcohol product is suggested on the basis of the apparent amounts of cationic products formed in the hydroxylation of 3. This pathway for cation production appears to require that the activated enzyme complex (equivalent to enzyme-substrate-H2O2) oxidizes substrate before water dissociates to give an iron-oxo species.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/jocen_US
dc.relation.ispartofJournal of Organic Chemistryen_US
dc.titleA Substituted Hypersensitive Radical Probe for Enzyme-Catalyzed Hydroxylations: Synthesis of Racemic and Enantiomerically Enriched Forms and Application in a Cytochrome P450-Catalyzed Oxidationen_US
dc.typeArticleen_US
dc.identifier.emailToy, PH:phtoy@hkucc.hku.hken_US
dc.identifier.authorityToy, PH=rp00791en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/jo9712097-
dc.identifier.scopuseid_2-s2.0-0000456008en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0000456008&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume62en_US
dc.identifier.issue26en_US
dc.identifier.spage9114en_US
dc.identifier.epage9122en_US
dc.identifier.isiWOS:000071410200031-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridToy, PH=7006579247en_US
dc.identifier.scopusauthoridDhanabalasingam, B=6507346325en_US
dc.identifier.scopusauthoridNewcomb, M=7101865783en_US
dc.identifier.scopusauthoridHanna, IH=7005983527en_US
dc.identifier.scopusauthoridHollenberg, PF=7005863178en_US

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