Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/75775
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Type: Journal article
Title: Desaturation of alkylbenzenes by Cytochrome P450BM3 (CYP102A1)
Author: Whitehouse, C.
Bell, S.
Wong, L.
Citation: Chemistry: A European Journal, 2008; 14(35):10905-10908
Publisher: Wiley-V C H Verlag GMBH
Issue Date: 2008
ISSN: 0947-6539
1521-3765
Statement of
Responsibility: 
Christopher J. C. Whitehouse, Stephen G. Bell, and Luet-Lok Wong
Abstract: A 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.
Keywords: C[BOND]H activation
cytochromes
dehydrogenation
isotope effects
oxidase
Rights: © 2008 Wiley-VCH Verlag GmbH&Co. KGaA, Weinheim
DOI: 10.1002/chem.200801927
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Chemistry and Physics publications

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