Abstract
The intramolecular kinetic deuterium isotope effects (kH/kD = 4.6–4.9) determined in the H2O2-induced oxidation of the racemic and enantiomeric forms of α-monodeuterated veratryl alcohol catalysed by lignin peroxidase (LiP) are very similar to those determined in the oxidation of racemic α-monodeuterated veratryl alcohol promoted either by a LiP model compound (a water soluble iron porphyrin using m-chloroperbenzoic acid as the oxidant) (kH/kD = 4.2) or by potassium 12-tungstocobalt(III)ate, a genuine one-electron oxidant (kH/kD = 4.5). These results indicate that very likely veratryl alcohol radical cation, once generated by the LiP–H2O2 system, is released from the enzyme and is deprotonated by the medium.
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Schedule a callMore From: Journal of the Chemical Society, Perkin Transactions 2
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