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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 342586
Title Enzymatic Baeyer-Villiger oxidation of benzaldehydes
Author(s) Moonen, M.J.H.; Westphal, A.H.; Rietjens, I.M.C.M.; Berkel, W.J.H. van
Source Advanced Synthesis and Catalysis 347 (2005)7-8. - ISSN 1615-4150 - p. 1027 - 1034.
Department(s) Biochemistry
Sub-department of Toxicology
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) p-hydroxybenzoate hydroxylase - 4-hydroxyacetophenone monooxygenase - hydrogen-peroxide - cyclohexanone monooxygenases - pseudomonas-fluorescens - substrate-specificity - directed evolution - phenol hydroxylase - aromatic-compounds - crystal-structure
Abstract The selectivity of the chemical Baeyer-Villiger oxidation of benzaldehydes depends on steric and electronic factors, the type of oxidizing agent and the reaction conditions. Here we report on the enzymatic Baeyer-Villiger oxidation of fluorobenzaldehydes as catalyzed by the flavoprotein 4-hydroxyacetophenone monooxygenase (HAPMO). HAPMO was most active with 4-amino- and 4-hydroxybenzaldehydes. With these compounds significant substrate inhibition occurred. Monofluoro- and difluorobenzaldehydes were readily oxidized by HAPMO without substrate inhibition. 19F NMR analysis revealed that 4-fluoro-, 2,6-difluoro-, 3,4-difluoro-, 2-fluoro-4-hydroxy- and 3-fluoro-4-hydroxybenzaldehyde were quantitatively converted by HAPMO to the corresponding fluorophenyl formates. These products spontaneously hydrolyzed to fluorophenols. The HAPMO-mediated conversion of 2-fluoro-, 3-fluoro-, 2,3-difluoro- and 2,4-difluorobenzaldehyde yielded, besides fluorophenols, also minor amounts of fluorobenzoic acids. The high preference of HAPMO for the production of fluorophenols is in disagreement with the rule derived from chemical studies that electron-poor benzaldehydes form mainly benzoic acids. This suggests that interactions of the benzaldehyde substrates with amino acids and/or the flavin cofactor in the enzyme active site influence the selection of the migratory group in favor of the phenyl ring
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