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FEBS Lett. 1998 May 29;428(3):141-6.

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

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FG Microbial Ecology, Technical University of Berlin, Germany.


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.

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