Mechanistic Insights into DyPB from Rhodococcus jostii RHA1 Via Kinetic Characterization
Author:
Affiliation:
1. Department of Chemistry, Kansas State University, Manhattan, Kansas 66506, United States
2. Department of Microbiology and Immunology, The University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada
Funder
Division of Chemistry
Canada Research Chairs
Natural Sciences and Engineering Research Council of Canada
Johnson Cancer Center
Publisher
American Chemical Society (ACS)
Subject
Catalysis,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acscatal.1c00703
Reference64 articles.
1. DyP-type peroxidases: a promising and versatile class of enzymes
2. The multihued palette of dye-decolorizing peroxidases
3. DyP-type peroxidases comprise a novel heme peroxidase family
4. Identification of DypB from Rhodococcus jostii RHA1 as a Lignin Peroxidase
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