A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta

FEBS Lett. 1998 May 29;428(3):141-6. doi: 10.1016/s0014-5793(98)00512-2.


A novel peroxidase, oxidizing Mn2+ and different aromatic compounds, was isolated. Hydroquinones, substituted phenols, dyes, other aromatic compounds and Mn2+ were compared as reducing substrates, and conclusions presented in the light of a molecular model built by homology modeling. The enzymes showed the fastest reaction rates with Mn2+, but the highest affinity corresponded to hydroquinones and dyes. Oxidation of Reactive Black 5 (an azo-dye not oxidized by Mn3+) was non-competitively inhibited by Mn2+. These findings, together with identification of putative Mn-binding site (involving Glu36, Glu40, Asp175 and inner heme propionate) and long-range electron transfer pathways, indicate that different sites are involved in substrate oxidation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Basidiomycota / enzymology*
  • Binding Sites
  • Chromatography, Ion Exchange
  • Heme
  • Hydrocarbons, Aromatic / metabolism
  • Kinetics
  • Manganese / metabolism
  • Models, Molecular
  • Peroxidases / chemistry
  • Peroxidases / isolation & purification
  • Peroxidases / metabolism*
  • Polyporaceae / enzymology*
  • Protein Conformation
  • Substrate Specificity


  • Hydrocarbons, Aromatic
  • Heme
  • Manganese
  • Peroxidases
  • manganese peroxidase