The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Crystal structures of dye‐decolorizing peroxidase with ascorbic acid and 2,6‐dimethoxyphenol
Abstract
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.
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“Although their action mechanism resembles that of other peroxidases, anthraquinone dye degradation is not yet fully mapped 129-134 .”
From Degradation of anthraquinone dyes from effluents: A review focusing on enzymatic dye degradation with industrial potential (2020) · cites this paper as [134]
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Porphyrins and Metalloporphyrins
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Nelson, D. P., & Kiesow, L. A. (1972) · Analytical Biochemistry · doi:10.1016/0003-2697(72)90451-4 · Cited by 925
Identification by ENDOR of Trp 191 as the Free-Radical Site in Cytochrome c Peroxidase Compound ES
Sivaraja, M., Goodin, D. B., Smith, M., & Hoffman, B. M. (1989) · Science · doi:10.1126/science.2549632 · Cited by 479
Structural basis of enzyme encapsulation into a bacterial nanocompartment
Sutter, M., Boehringer, D., Gutmann, S., Günther, S., Prangishvili, D., Loessner, M. J., Stetter, K. O., Weber-Ban, E., & Ban, N. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1473 · Cited by 411
Kim, S. J., & Shoda, M. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.3.1029-1035.1999 · Cited by 274
DyP-type peroxidases comprise a novel heme peroxidase family
Sugano, Y. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8651-8 · Cited by 254
Self-citationTwo Substrate Interaction Sites in Lignin Peroxidase Revealed by Site-Directed Mutagenesis
Doyle, W. A., Blodig, W., Veitch, N. C., Piontek, K., & SMITH, A. T. (1998) · Biochemistry · doi:10.1021/bi981633h · Cited by 247
DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family
Sugano, Y., Muramatsu, R., Ichiyanagi, A., Sato, T., & Shoda, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706996200 · Cited by 222
Self-citationLiers, C., Bobeth, C., Pecyna, M. J., Ullrich, R., & Hofrichter, M. (2009) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-009-2173-7 · Cited by 210
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- K.M. Smith J.H. Fuhrhop 1975 Elsevier Amsterdam
Cited by
Routoula, E., & Patwardhan, S. V. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.9b03737 · Cited by 579
Metadata
- Authors
- Yoshida, T., Tsuge, H., Hisabori, T., & Sugano, Y.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2012-11-15
- Volume
- 586
- Issue
- 24
- Pages
- 4351-4356
- ISSN
- 0014-5793
- 1873-3468
- Cited by
- 46
- References
- 29
- Language
- en
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- Yoshida, T., Tsuge, H., Hisabori, T., & Sugano, Y. (2012). Crystal structures of dye‐decolorizing peroxidase with ascorbic acid and 2,6‐dimethoxyphenol. FEBS Letters. https://doi.org/10.1016/j.febslet.2012.10.049
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