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- W2008754081 abstract "The mushroom Agrocybe aegerita secretes a peroxidase (AaP) that catalyzes halogenations and hydroxylations. Phenol was brominated to 2‐ and 4‐bromophenol (ratio 1:4) and chlorinated to a lesser extent to 2‐chlorophenol. The purified enzyme was found to oxidize toluene via benzyl alcohol and benzaldehyde into benzoic acid. A second fraction of toluene was hydroxylated to give p ‐cresol as well as o ‐cresol and methyl‐ p ‐benzoquinone. The UV–Vis absorption spectrum of purified AaP showed high similarity to a resting state cytochrome P450 with the Soret band at 420 nm and additional maxima at 278, 358, 541 and 571 nm; the AaP CO‐complex had a distinct absorption maximum at 445 nm that is characteristic for heme‐thiolate proteins. AaP regioselectively hydroxylated naphthalene to 1‐naphthol and traces of 2‐naphthol (ratio 36:1). H 2 O 2 was necessarily required for AaP function and hence the hydroxylations catalyzed by AaP can be designated as peroxygenation and the enzyme as an extracellular peroxygenase." @default.
- W2008754081 created "2016-06-24" @default.
- W2008754081 creator A5070236541 @default.
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- W2008754081 date "2005-10-19" @default.
- W2008754081 modified "2023-10-13" @default.
- W2008754081 title "The haloperoxidase of the agaric fungus<i>Agrocybe aegerita</i>hydroxylates toluene and naphthalene" @default.
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- W2008754081 doi "https://doi.org/10.1016/j.febslet.2005.10.014" @default.
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