Resonance Raman view of the active site architecture in bacterial DyP-type peroxidases
Author:
Affiliation:
1. Instituto de Tecnologia Química e Biológica António Xavier
2. Universidade NOVA de Lisboa
3. 2780-157 Oeiras
4. Portugal
5. Molecular Enzymology
6. University of Groningen
7. 9747AG Groningen
8. The Netherlands
Abstract
The solution active site architecture of DyPs, which is sensitively revealed by RR spectroscopy, is crucial for comprehension of their physiological roles and for evaluation of their potential for biotechnological application.
Funder
Fundação para a Ciência e a Tecnologia
European Regional Development Fund
Horizon 2020
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/RA/D0RA00950D
Reference45 articles.
1. DyP-type peroxidases comprise a novel heme peroxidase family
2. A structural and functional perspective of DyP-type peroxidase family
3. The multihued palette of dye-decolorizing peroxidases
4. Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study
5. DyP-type peroxidases: a promising and versatile class of enzymes
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1. Superoxide versus peroxide activation of dye decolorizing peroxidases for bioelectrocatalysis;Bioresource Technology Reports;2024-06
2. Biochemical, Biophysical, and Structural Analysis of an Unusual DyP from the Extremophile Deinococcus radiodurans;Molecules;2024-01-11
3. Direct Electrochemical Generation of Catalytically Competent Oxyferryl Species of Classes I and P Dye Decolorizing Peroxidases;International Journal of Molecular Sciences;2021-11-20
4. SERR Spectroelectrochemistry as a Guide for Rational Design of DyP-Based Bioelectronics Devices;International Journal of Molecular Sciences;2021-07-27
5. Electrocatalysis by Heme Enzymes—Applications in Biosensing;Catalysts;2021-02-06
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