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A study on reducing substrates of manganese‐oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta
Author(s) -
Heinfling Annette,
Ruiz-Dueñas Francisco Javier,
Martı́nez Marı́a J,
Bergbauer Matthias,
Szewzyk Ulrich,
Martı́nez Angel T
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00512-2
Subject(s) - chemistry , manganese peroxidase , pleurotus eryngii , oxidizing agent , peroxidase , manganese , heme , substrate (aquarium) , lignin peroxidase , phenols , electron transfer , photochemistry , enzyme , organic chemistry , biology , raw material , ecology
A novel peroxidase, oxidizing Mn 2+ and different aromatic compounds, was isolated. Hydroquinones, substituted phenols, dyes, other aromatic compounds and Mn 2+ 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 Mn 2+ , but the highest affinity corresponded to hydroquinones and dyes. Oxidation of Reactive Black 5 (an azo‐dye not oxidized by Mn 3+ ) was non‐competitively inhibited by Mn 2+ . These findings, together with identification of putative Mn‐binding site (involving Glu 36 , Glu 40 , Asp 175 and inner heme propionate) and long‐range electron transfer pathways, indicate that different sites are involved in substrate oxidation.