Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 193, Issue -, Pages 601-608Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2021.10.100
Keywords
Dye-decolorizing peroxidase; Crystal structure; Veratryl alcohol
Funding
- DBT
- Of India, Ministry of Science and Technology [BT/PR20463/BCE/8/1387/2016]
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This study delves into the oxidation reactions of veratryl alcohol (VA), 2,6-dimethoxyphenol (DMP), and guaiacol by Dye-decolorizing peroxidases (DyPs), revealing their comparable binding affinity and assisting in modulating BsDyP's structure engineering for enhanced activity towards a wide range of substrates.
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 0.065 s(-1), followed by the oxidation of 2,6-dimethoxyphenol (DMP) and guaiacol with a comparable turnover number (k(cat)) of 0.07 s(-1) and 0.07 s(-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.
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