Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation |
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Authors: | Martin Kluge René Ullrich Christoph Dolge Katrin Scheibner Martin Hofrichter |
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Affiliation: | (1) Unit of Environmental Biotechnology, International Graduate School of Zittau, Zittau, Germany;(2) University of Applied Sciences Lausitz, Senftenberg, Germany |
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Abstract: | 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. |
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Keywords: | Peroxidase Oxygenation Hydroxylation P450 Naphthol |
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