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Article: Oxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath)

TitleOxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
Authors
Issue Date1999
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1999, v. 274 n. 16, p. 10771-10776 How to Cite?
AbstractRadical clock substrate probes were used to assess the viability of a discrete substrate radical species in the mechanism of hydrocarbon oxidation by the soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath). New substituted cyclopropane probes were used with very fast ring- opening rate constants and other desirable attributes, such as the ability to discriminate between radical and cationic intermediates. Oxidation of these substrates by a reconstituted sMMO system resulted in no rearranged products, allowing an upper limit of 150 fs to be placed on the lifetime of a putative radical species. This limit strongly suggests that there is no such substrate radical intermediate. The two enantiomers of trans-1-methyl-2- phenylcyclopropane were prepared, and the regioselectivity of their oxidation to the corresponding cyclopropylmethanol and cyclopropylphenol products was determined. The results are consistent with selective orientation of the two enantiomeric substrates in the hydrophobic cavity at the active site of sMMO, specific models for which were examined by molecular modeling.
Persistent Identifierhttp://hdl.handle.net/10722/167628
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorValentine, AMen_US
dc.contributor.authorLetadicBiadatti, MHen_US
dc.contributor.authorToy, PHen_US
dc.contributor.authorNewcomb, Men_US
dc.contributor.authorLippard, SJen_US
dc.date.accessioned2012-10-08T03:09:14Z-
dc.date.available2012-10-08T03:09:14Z-
dc.date.issued1999en_US
dc.identifier.citationJournal Of Biological Chemistry, 1999, v. 274 n. 16, p. 10771-10776en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/167628-
dc.description.abstractRadical clock substrate probes were used to assess the viability of a discrete substrate radical species in the mechanism of hydrocarbon oxidation by the soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath). New substituted cyclopropane probes were used with very fast ring- opening rate constants and other desirable attributes, such as the ability to discriminate between radical and cationic intermediates. Oxidation of these substrates by a reconstituted sMMO system resulted in no rearranged products, allowing an upper limit of 150 fs to be placed on the lifetime of a putative radical species. This limit strongly suggests that there is no such substrate radical intermediate. The two enantiomers of trans-1-methyl-2- phenylcyclopropane were prepared, and the regioselectivity of their oxidation to the corresponding cyclopropylmethanol and cyclopropylphenol products was determined. The results are consistent with selective orientation of the two enantiomeric substrates in the hydrophobic cavity at the active site of sMMO, specific models for which were examined by molecular modeling.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCatalysisen_US
dc.subject.meshFree Radicalsen_US
dc.subject.meshKineticsen_US
dc.subject.meshMethylococcaceae - Enzymologyen_US
dc.subject.meshMolecular Probesen_US
dc.subject.meshOxidation-Reductionen_US
dc.subject.meshOxygenases - Metabolismen_US
dc.subject.meshSolubilityen_US
dc.subject.meshSubstrate Specificityen_US
dc.titleOxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath)en_US
dc.typeArticleen_US
dc.identifier.emailToy, PH:phtoy@hkucc.hku.hken_US
dc.identifier.authorityToy, PH=rp00791en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1074/jbc.274.16.10771en_US
dc.identifier.pmid10196150-
dc.identifier.scopuseid_2-s2.0-0033574674en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033574674&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume274en_US
dc.identifier.issue16en_US
dc.identifier.spage10771en_US
dc.identifier.epage10776en_US
dc.identifier.isiWOS:000079751900018-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridValentine, AM=7006314722en_US
dc.identifier.scopusauthoridLeTadicBiadatti, MH=6506838634en_US
dc.identifier.scopusauthoridToy, PH=7006579247en_US
dc.identifier.scopusauthoridNewcomb, M=7101865783en_US
dc.identifier.scopusauthoridLippard, SJ=35431416600en_US

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