Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation
- Agrocybe aegerita peroxidase/peroxygenase (AaP) is an extracellular fungal biocatalyst that selectively hydroxylates the aromatic ring of naphthalene. Under alkaline conditions, the reaction proceeds via the formation of an intermediary product with a molecular mass of 144 and a characteristic UV absorption spectrum (A max 210, 267, and 303 nm). The compound was semistable at pH 9 but spontaneously hydrolyzed under acidic conditions (pH <7) into 1-naphthol as major product and traces of 2-naphthol. Based on these findings and literature data, we propose naphthalene 1,2-oxide as the primary product of AaP-catalyzed oxygenation of naphthalene. Using 18O-labeled hydrogen peroxide, the origin of the oxygen atom transferred to naphthalene was proved to be the peroxide that acts both as oxidant (primary electron acceptor) and oxygen source.
Author: | Martin Kluge, René UllrichORCiD, Christoph Dolge, Katrin Scheibner, Martin HofrichterORCiD |
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URL: | http://link.springer.com/article/10.1007%2Fs00253-008-1704-y |
DOI: | https://doi.org/10.1007/s00253-008-1704-y |
ISSN: | 0175-7598 |
Title of the source (English): | Applied Microbiology and Biotechnology |
Document Type: | Scientific journal article peer-reviewed |
Language: | English |
Year of publication: | 2009 |
Tag: | Hydroxylation; Naphthol; Oxygenation; P450; Peroxidase |
Volume/Year: | 81 |
Issue number: | 6 |
First Page: | 1071 |
Last Page: | 1076 |
Faculty/Chair: | Fakultät 2 Umwelt und Naturwissenschaften / FG Enzymtechnologie |
Institution name at the time of publication: | Fakultät für Naturwissenschaften (eHL) / Prof. Enzymtechnologie |