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Total records: 126
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[ 2013 ] Churakova E, Arends IWCE, Hollmann F Increasing the Productivity of Peroxidase-Catalyzed Oxyfunctionalization: A Case Study on the Potential of Two-Liquid-Phase Systems ChemCatChem, 5: 565-568

[ 2013 ] Hahn F, Ullrich R, Hofrichter M, Liers C Experimental approach to follow the spatiotemporal wood degradation in fungal microcosms Biotechnol. J., 8: 127-132

[ 2013 ] Karich A, Kluge M, Ullrich R, Hofrichter M Benzene oxygenation and oxidation by the peroxygenase of Agrocybe aegerita AMB Express, 3: 5-13

[ 2013 ] Kluge M, Ullrich R, Scheibner K, Hofrichter M Formation of naphthalene hydrates in the enzymatic conversion of 1,2-dihydronaphthalene by two fungal peroxygenases and subsequent naphthalene formation J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.08.017

[ 2013 ] Liers C, Aranda E, Strittmatter E, Piontek K, Plattner D, Zorn H, Ullrich R, Hofrichter M Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.09.025

[ 2013 ] Liers C, Pecyna MJ, Kellner H, Worrich A, Zorn H, Steffen KT, Hofrichter M, Ullrich R Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases Appl. Microbiol. Biotechnol., 97: 5839-5849

DyP-type peroxidases (DyP = dye decolorizing peroxidases) belong to the large group of heme peroxidases. They utilize hydrogen peroxide to catalyze oxidations of various organic compounds. AauDyPI from Auricularia auricula-judae (Fungi) was crystallized and its crystal structure was determined at 2.1 A resolution. The mostly helical structure also shows a beta-sheet motif typical for DyPs and Cld-related structures and includes the complete poypeptide chain. At the distal side of the heme molecule, a flexible aspartate residue (Asp168) plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterwards, its side chain changes its conformation now pointing toward the protein backbone. We propose an extended functionality of Asp168, that acts like a gatekeeper by altering the width of the heme cavity access channel. Chemical modifications of potentially redox-active amino acids show that a tyrosine is involved in substrate interaction. Using spin trapping experiments a transient radical on the surface-exposed Tyr337 was identified as the oxidation site for bulky substrates. A possible long-range electron transfer (LRET) pathway from the surface of the enzyme to the redox cofactor (heme) is discussed.