Identification of Surface-Exposed Protein Radicals and A Substrate Oxidation Site in A-Class Dye-Decolorizing Peroxidase from Thermomonospora curvata-Reference-Cited by-同舟云学术

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Identification of Surface-Exposed Protein Radicals and A Substrate Oxidation Site in A-Class Dye-Decolorizing Peroxidase from Thermomonospora curvata

Published:2016-10-31 Issue:12 Volume:6 Page:8036-8047
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Shrestha Ruben,Chen Xuejie,Ramyar Kasra X.,Hayati Zahra¹,Carlson Eric A.,Bossmann Stefan H.,Song Likai¹,Geisbrecht Brian V.,Li Ping

Affiliation:

1. National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, United States

Funder

National Institute of Allergy and Infectious Diseases

National Institute of General Medical Sciences

Johnson Cancer Research Center, Kansas State University

National High Magnetic Field Laboratory

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.6b01952

Reference51 articles.

1. The multihued palette of dye-decolorizing peroxidases

2. DyP-type peroxidases: a promising and versatile class of enzymes

3. Purification and Characterization of a Novel Peroxidase from Geotrichum candidum Dec 1 Involved in Decolorization of Dyes

4. Insights into Lignin Degradation and its Potential Industrial Applications

5. Lignin-degrading enzymes

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3. Engineering A‐type Dye‐Decolorizing Peroxidases by Modification of a Conserved Glutamate Residue;ChemBioChem;2024-04-08

4. Dye-decolorizing peroxidase of Thermobifida halotolerance displays complex kinetics with both substrate inhibition and apparent positive cooperativity;Archives of Biochemistry and Biophysics;2024-04

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