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Dye-decolorizing peroxidases (DyPs) represent a novel family of heme peroxidases that use H2O2 as the final electron acceptor to catalyze the oxidation of various organic compounds. A DyP from Irpex lacteus F17 (Il-DyP4, corresponding to GenBank MG209114), obtained by heterologous expression, exhibits a high catalytic efficiency for phenolic compounds and a strong decolorizing ability toward various synthetic dyes. However, the enzyme structure and the catalytic residues involved in substrate oxidation remain poorly understood. Here, we obtained a high-resolution structure (2.0 Å, PDB: 7D8M) of Il‑DyP4 with α-helices, anti-parallel β-sheets and one ferric heme cofactor sandwiched between two domains. The crystal structure of Il‑DyP4 revealed two heme access channels leading from the enzyme molecular surface to its heme region, and also showed four conserved amino acid residues forming the pocket for the conversion of hydrogen peroxide into the water mole
Nature News: Chaga a forest fungus that fights cancer
By Susan Pike
I love the idea of foraging for mushrooms, but rarely do it. There are two reasons for this, I worry about overharvesting. Nature is so stressed out by us as is, it doesn’t help to have us rooting around collecting plants and fungi that we don’t truly need to survive. I’m not anti-foraging. There are sustainable ways to harvest. I just like to be sure I’m going to use whatever I collect and that there is plenty of it to go around. My second reason is that I don’t have enough training to be absolutely sure about the identity of the mushrooms I’m collecting. There is, however, one member of the Fungi Kingdom that I can confidently identify and finding it in the woods is like finding an old friend - the chaga (scientific name Inonotus obliquus).