Oxidation of Rotenone by Polyporus anceps Laccase

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Abstract
The extracellular laccase produced by Polyporus anceps transforms rotenone to a single, more polar product. This transformation occurs in incubation mixtures containing chlorpromazine, laccase and rotenone where rotenone serves as a pseudosubstrate for the enzyme. Chlorpromazine, the true substrate, serves as a cycling redox component of the system forming a radical-cation species that abstracts an electron from rotenone in the oxidation process. Physicochemical properties of the product were determined on an analytically pure sample obtained by preparative hplc [high-performance liquid chromatography]. High resolution ms [mass spectrometry], high-field PMR and cmr [carbon magnetic resonance], and optical rotation analyses indicated that rotenone was transformed to 6a.beta., 12a.beta.-rotenolone by P. anceps laccase. [Rotenone is a widely used pesticide. The compound possesses a range of biological activities, including its ability to induce neoplastic, paraneoplastic and preneoplastic lesions in rats.].

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