TY - GEN A1 - Kluge, Martin A1 - Ullrich, René A1 - Scheibner, Katrin A1 - Hofrichter, Martin T1 - Spectrophotometric assay for detection of aromatic hydroxylation catalyzed by fungal haloperoxidase–peroxygenase T2 - Applied Microbiology and Biotechnology N2 - Agrocybe aegerita peroxidase (AaP) is a versatile heme-thiolate protein that can act as a peroxygenase and catalyzes, among other reactions, the hydroxylation of aromatic rings. This paper reports a rapid and selective spectrophotometric method for directly detecting aromatic hydroxylation by AaP. The weakly activated aromatic compound naphthalene served as the substrate that was regioselectively converted into 1-naphthol in the presence of the co-substrate hydrogen peroxide. Formation of 1-naphthol was followed at 303 nm (ɛ 303 = 2,010 M−1 cm−1), and the apparent Michaelis–Menten (K m) and catalytic (k cat) constants for the reaction were estimated to be 320 μM and 166 s−1, respectively. This method will be useful in screening of fungi and other microorganisms for extracellular peroxygenase activities and in comparing and assessing different catalytic activities of haloperoxidase–peroxygenases. KW - Hydroxylation KW - Peroxygenase Y1 - 2014 UR - https://opus4.kobv.de/opus4-UBICO/frontdoor/index/index/docId/11661 UR - http://link.springer.com/article/10.1007%2Fs00253-007-0942-8 SN - 1432-0614 VL - 75 IS - 6 SP - 1473 EP - 1478 ER -