Oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium Involvement of activated oxygen

AbstractThe oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium was studied. Five products were identified: veratraldehyde, two quinones and two aromatic ring cleavage lactones. A similar product pattern was obtained with the 1-electron oxidant cerium(IV). Under anaerobic reaction conditions or in the presence of Mn(II) only traces of quinones or lactones were detected besides veratraldehyde. This indicates the involvement of activated oxygen species in the enzyme reaction. Possible mechanisms for the formation of the primary oxidation products from veratryl alcohol are discussed