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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 |
Published version: | http://dx.doi.org/10.1002/chem.200801927 |
Appears in Collections: | Aurora harvest 4 Chemistry and Physics publications |
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