Optimized oxidoreductases for medium and large scale industrial biotransformations
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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
year2013
First Crystal Structure of a Fungal High-Redox Potential Dye-decolorizing Peroxidase: Substrate Interaction Sites and Long-Range Electron Transfer
Strittmatter E, Liers C, Ullrich R, Wachter S, Hofrichter M, Plattner D, Piontek K
J. Biol. Chem., 288: 4095-4102
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.
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[ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by
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