Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/75775
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dc.contributor.authorWhitehouse, C.-
dc.contributor.authorBell, S.-
dc.contributor.authorWong, L.-
dc.date.issued2008-
dc.identifier.citationChemistry: A European Journal, 2008; 14(35):10905-10908-
dc.identifier.issn0947-6539-
dc.identifier.issn1521-3765-
dc.identifier.urihttp://hdl.handle.net/2440/75775-
dc.description.abstractA study was conducted to investigate the desaturation of alkylbenezenes by cytochrome P450BM3 (CYP102A1). It was observed during the study that oxidation of alkylbenzenes with CYP102A1 involves a gamut of P450 activity types that are terminal, sub-terminal benzylic and aromatic hydroxylation; terminal and sub-terminal desaturation; and epoxidation of the olefins. It was also found that the desaturation of cumene by CYP102A1 is sensitive to α-deuteration and insensitive to β-deuteration. Intramolecular deuterium isotope study revealed that the first abstraction in the desaturation of valproic acid and ezlopitant by microsomal P450s take place from activated carbon atoms. The increased β-hydroxylation percentages show that the β-carbon lies closer to the ferryl oxygen in the KT5.-
dc.description.statementofresponsibilityChristopher J. C. Whitehouse, Stephen G. Bell, and Luet-Lok Wong-
dc.language.isoen-
dc.publisherWiley-V C H Verlag GMBH-
dc.rights© 2008 Wiley-VCH Verlag GmbH&Co. KGaA, Weinheim-
dc.subjectC[BOND]H activation-
dc.subjectcytochromes-
dc.subjectdehydrogenation-
dc.subjectisotope effects-
dc.subjectoxidase-
dc.titleDesaturation of alkylbenzenes by Cytochrome P450BM3 (CYP102A1)-
dc.typeJournal article-
dc.identifier.doi10.1002/chem.200801927-
pubs.publication-statusPublished-
dc.identifier.orcidBell, S. [0000-0002-7457-9727]-
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Chemistry and Physics publications

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