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Total records: 126
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[ 2013 ] Salvachúa D, Martínez AT, Tien M, López-Lucendo MF, García F, de los Ríos V, Martínez MJ, Prieto A Differential proteomic analysis of the secretome of Irpex lacteus and other white-rot fungi during wheat straw pretreatment Biotechnol. Biofuels, 6: 115-129

[ 2013 ] Salvachúa D, Prieto A, Mattinen ML, Tamminen T, Liitiä T, Lille M, Willför S, Martínez AT, Martínez MJ, Faulds CB Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking Enz. Microb. Technol., 52: 303-311

[ 2013 ] Strittmatter E, Liers C, Ullrich R, Wachter S, Hofrichter M, Plattner D, Piontek K First Crystal Structure of a Fungal High-Redox Potential Dye-decolorizing Peroxidase: Substrate Interaction Sites and Long-Range Electron Transfer J. Biol. Chem., 288: 4095-4102

[ 2013 ] Strittmatter E, Wachter S, Liers C, Ullrich R, Hofrichter M, Plattner D, Piontek K Radical formation on a conserved tyrosine residue is crucial for DyP activity Arch. Biochem. Biophys., 537: 161-167

[ 2013 ] Turbe-Doan A, Arfi Y, Record E, Estrada-Alvarado I, Levasseur A Heterologous production of cellobiose dehydrogenases from the basidiomycete Coprinopsis cinerea and the ascomycete Podospora anserina and their effect on saccharification of wheat straw Appl. Microbiol. Biotechnol., 97: 4873-4885

[ 2013 ] Wang X, Peter S, Ullrich R, Hofrichter M, Groves JT Driving Force for Oxygen-Atom Transfer by Heme-Thiolate Enzymes Angew. Chem. Int. Ed., 52: 9238-9241

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.