Mechanism of non-phenolic substrate oxidation by the fungal laccase Type 1 copper site from Trametes versicolor: the case of benzo[ a]pyrene and anthracene

Dalton Trans. 2024 Jul 23;53(29):12152-12161. doi: 10.1039/d4dt01377h.

Abstract

Laccases (EC 1.10.3.2) are multicopper oxidases with the capability to oxidize diverse phenolic and non-phenolic substrates. While the molecular mechanism of their activity towards phenolic substrates is well-established, their reactivity towards non-phenolic substrates, such as polycyclic aromatic hydrocarbons (PAHs), remains unclear. To elucidate the oxidation mechanism of PAHs, particularly the activation mechanism of the sp2 aromatic C-H bond, we conducted a density functional theory investigation on the oxidation of two PAHs (anthracene and benzo[a]pyrene) using an extensive model of the T1 copper catalytic site of the fungal laccase from Trametes versicolor.

MeSH terms

  • Anthracenes* / chemistry
  • Anthracenes* / metabolism
  • Benzo(a)pyrene* / chemistry
  • Benzo(a)pyrene* / metabolism
  • Catalytic Domain
  • Copper* / chemistry
  • Copper* / metabolism
  • Density Functional Theory
  • Laccase* / chemistry
  • Laccase* / metabolism
  • Models, Molecular
  • Oxidation-Reduction*
  • Polyporaceae / enzymology
  • Polyporales / enzymology
  • Polyporales / metabolism
  • Trametes / enzymology

Substances

  • Laccase
  • Anthracenes
  • anthracene
  • Copper
  • Benzo(a)pyrene

Supplementary concepts

  • Trametes versicolor