@misc{KlugeUllrichDolgeetal., author = {Kluge, Martin and Ullrich, Ren{\´e} and Dolge, Christoph and Scheibner, Katrin and Hofrichter, Martin}, title = {Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation}, series = {Applied Microbiology and Biotechnology}, volume = {81}, journal = {Applied Microbiology and Biotechnology}, number = {6}, issn = {0175-7598}, doi = {10.1007/s00253-008-1704-y}, pages = {1071 -- 1076}, 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.}, language = {en} }