Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor
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Author (Corporation)
Publication date
2023
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Course of study
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Type
01A - Journal article
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Parent work
Chemical Communications
Special issue
DOI of the original publication
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Series
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Volume
59
Issue / Number
62
Pages / Duration
Patent number
Publisher / Publishing institution
Royal Society of Chemistry
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Abstract
Metal complexes introduced into esterase enzyme scaffolds can generate versatile biomimetic catalysts endowed with oxidoreductase activity.
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ISBN
ISSN
1359-7345
1364-548X
0009-241X
1364-548X
0009-241X
Language
English
Created during FHNW affiliation
Yes
Strategic action fields FHNW
Publication status
Published
Review
Peer review of the complete publication
Open access category
Hybrid
Citation
Fernandez-Lopez, L., Cea-Rama, I., Alvarez-Malmagro, J., Ressmann, A. K., Gonzalez-Alfonso, J. L., Coscolín, C., Shahgaldian, P., Plou, F. J., Modregger, J., Pita, M., Sanz-Aparicio, J., & Ferrer, M. (2023). Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor. Chemical Communications, 59(62). https://doi.org/10.1039/D3CC01946B