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

FEBS Letters

Martı́nez, Marı́a J¹  Bergbauer, Matthias²  Ruiz-Dueñas, Francisco Javier¹  Heinfling, Annette²  Martı́nez, Angel T¹  Szewzyk, Ulrich² 

[1] Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Cientı́ficas (C.S.I.C.), Velázquez 144, E-28006 Madrid, Spain;FG Microbial Ecology, Technical University of Berlin, Sekr. OE5, Franklinstrasse 29, D-10587 Berlin, Germany

关键词: Peroxidase;    Manganese;    Hydroquinone;    Dye;    Substrate binding site;    Ligninolytic fungus;   

DOI  :  10.1016/S0014-5793(98)00512-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown