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Publication Abstract from PubMed

Dye-decolorizing peroxidases (DyPs) are heme-containing peroxidases, which have promising application in biodegradation of phenolic lignin compounds and in detoxification of dyes. In this study, the crystal structure of BsDyP- veratryl alcohol (VA) complex delves deep into the binding of small substrate molecules within the DyP heme cavity. The biochemical analysis shows that BsDyP oxidizes the VA with a turnover number of 0.065s(-1), followed by the oxidation of 2,6-dimethoxyphenol (DMP) and guaiacol with a comparable turnover number (kcat) of 0.07s(-1) and 0.07s(-1), respectively. Moreover, biophysical and computational studies reveal the comparable binding affinity of substrates to BsDyP and produce lower-energy stable BsDyP-ligand(s) complexes. All together with our previous findings, we are providing a complete structural description of substrate-binding sites in DyP. The structural insight of BsDyP helps to modulate its engineering to enhance the activity towards the oxidation of a wide range of substrates.

Structure of dye-decolorizing peroxidase from Bacillus subtilis in complex with veratryl alcohol.,Dhankhar P, Dalal V, Singh V, Sharma AK, Kumar P Int J Biol Macromol. 2021 Oct 20. pii: S0141-8130(21)02258-3. doi:, 10.1016/j.ijbiomac.2021.10.100. PMID:34687768^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.