Electrochemical Actuation of a DyP Peroxidase: A Facile Method for Drastic Improvement of the Catalytic Performance-Reference-Cited by-同舟云学术

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Electrochemical Actuation of a DyP Peroxidase: A Facile Method for Drastic Improvement of the Catalytic Performance

Published:2023-05-18 Issue:11 Volume:13 Page:7437-7449
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Scocozza Magalí F.¹²^ORCID,Vieyra Francisco¹²,Battaglini Fernando¹²^ORCID,Martins Ligia O.³^ORCID,Murgida Daniel H.¹²^ORCID

Affiliation:

1. Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, Argentina

2. Instituto de Química Física de Los Materiales, Medio Ambiente y Energía (INQUIMAE), CONICET-Universidad de Buenos Aires, Buenos Aires C1428EGA, Argentina

3. Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras 2780-157, Portugal

Funder

H2020 Marie Sklodowska-Curie Actions

Universidad de Buenos Aires

Fondo para la Investigaci?n Cient?fica y Tecnol?gica

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.3c01530

Reference56 articles.

1. DyP-type peroxidases comprise a novel heme peroxidase family

2. DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family

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

4. DyP-Type Peroxidases: Recent Advances and Perspectives

5. Dye Decoloring Peroxidase Structure, Catalytic Properties and Applications: Current Advancement and Futurity

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Evaluation of a dye-decolorizing peroxidase from Comamonas serinivorans for lignin valorization potentials;International Journal of Biological Macromolecules;2023-12

2. Heterologous expression, purification and structural features of native Dictyostelium discoideum dye-decolorizing peroxidase bound to a natively incorporated heme;Frontiers in Chemistry;2023-08-01

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