Fungal peroxygenases are extracellular heme-thiolate biocatalysts that mediate the selective oxygenation of a variety of substrates using hydrogen peroxide as a co-substrate. Little is known about the physiological role or the catalytic mechanism of these enzymes. We have found that the peroxygenase secreted by Agrocybe aegerita catalyzes the H2O2-dependent hydroxylation of alkanes with high efficiency. The hydroxylation of cyclohexane mediated by H218O2 resulted in complete incorporation of 18O into the hydroxyl group of the product cyclohexanol. The hydroxylation of partially deuterated n-hexane revealed a large intramolecular deuterium isotope effect of 16. Hydroxylation of the diagnostic substrate norcarane indicated a radical rebound hydroxylation mechanism with a radical lifetime of 9.4 ps and an oxygen rebound rate of 1011 s-1.Cf. FEBS J., 2011 , 278, 3667-3675; DOI: 10.1111/j.1742-4658.2011.08285.x.

Selective hydroxylation of alkanes by APO: An extracellular fungal heme-thiolate peroxygenase

243rd National Meeting (2012)

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