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Crystal structures of dye‐decolorizing peroxidase with ascorbic acid and 2,6‐dimethoxyphenol
Author(s) -
Yoshida Toru,
Tsuge Hideaki,
Hisabori Toru,
Sugano Yasushi
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.10.049
Subject(s) - peroxidase , heme , ascorbic acid , chemistry , substrate (aquarium) , hydrogen bond , propionate , stereochemistry , cytochrome c peroxidase , molecule , enzyme , biochemistry , organic chemistry , biology , ecology , food science
The structure of dye‐decolorizing peroxidase (DyP)‐type peroxidase differs from that of other peroxidase families, indicating that DyP‐type peroxidases have a different reaction mechanism. We have determined the crystal structures of DyP with ascorbic acid and 2,6‐dimethoxyphenol at 1.5 and 1.4 Å, respectively. The common binding site for both substrates was located at the entrance of the second cavity leading from the DyP molecular surface to heme. This resulted in a hydrogen bond network connection between each substrate and the heme distal side. This network consisted of water molecules occupying the second cavity, heme 6‐propionate, Arg329, and Asn313. This network is consistent with the proton transfer pathway from substrate to DyP.