Abstract
The mechanism of C-C and ether bond cleavages of Cα- or Cβ-deuterated β-O-4 and β-1 lignin substructure models and the vicinal diol compounds catalyzed by the enzyme system from Phanerochaete chrysosporium culture was investigated. The enzymatic oxidation of β-O-4 lignin model compounds in the presence of H2O2 and O2 yielded C6-Cα-derived benzaldehyde, and Cβ-Cγ-derived product together with the arylglycerol product. Likewise, the β-1 models and the diol compounds also underwent the C-C bond cleavage, yielding C6-Cα-derived benzaldehyde and the arylglycol product. The results demonstrated that the D-labels at Cα and Cβ of the substrates were retained in the products after the Cα-Cβ and ether bond cleavages.
