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Spectrophotometric assay for detection of aromatic hydroxylation catalyzed by fungal haloperoxidase–peroxygenase

  • 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.

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Author: Martin Kluge, René UllrichORCiD, Katrin Scheibner, Martin HofrichterORCiD
URL:http://link.springer.com/article/10.1007%2Fs00253-007-0942-8
DOI:https://doi.org/10.1007/s00253-007-0942-8
ISSN:1432-0614
Title of the source (English):Applied Microbiology and Biotechnology
Document Type:Scientific journal article peer-reviewed
Language:English
Year of publication:2007
Tag:Hydroxylation; Peroxygenase
Volume/Year:75
Issue number:6
First Page:1473
Last Page:1478
Faculty/Chair:Fakultät 2 Umwelt und Naturwissenschaften / FG Enzymtechnologie
Institution name at the time of publication:Fakultät für Naturwissenschaften (eHL) / Prof. Enzymtechnologie
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