Abstract
Lignin peroxidase catalyses the H 2O 2-induced oxidation of 4-methoxybenzyltrimethylsilane by an electron transfer mechanism. The intermediate radical cation undergoes preferentially C α–H deprotonation to give 4-methoxybenzaldehyde whereas C α–Si bond cleavage is a minor fragmentation pathway and leads to 4-methoxybenzyl alcohol. Similar results are obtained in the oxidation catalysed by the water soluble model compound 5,10,15,20-tetra( N-methyl-4-pyridyl)porphyrinatoiron(III) pentachloride. Instead, in the oxidation promoted by the genuine one-electron transfer oxidant potassium dodecatungstocobalt(III)ate C α–Si bond cleavage is the exclusive fragmentation process of the intermediate radical cation. It is suggested that in the enzymatic and biomimetic oxidations of 4-methoxybenzyltrimethylsilane the deprotonation of the intermediate radical cation is promoted by the reduced form [PorFe(IV)O] of the active oxidant, which is an iron-oxo porphyrin radical cation.
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