TY - GEN A1 - Kluge, Martin A1 - Ullrich, René A1 - Dolge, Christoph A1 - Scheibner, Katrin A1 - Hofrichter, Martin T1 - Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation T2 - Applied Microbiology and Biotechnology N2 - 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. KW - Peroxidase KW - Oxygenation KW - Hydroxylation KW - P450 KW - Naphthol Y1 - 2009 UR - http://link.springer.com/article/10.1007%2Fs00253-008-1704-y U6 - https://doi.org/10.1007/s00253-008-1704-y SN - 0175-7598 VL - 81 IS - 6 SP - 1071 EP - 1076 ER -