Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor

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Transforming_an_esterase.pdf(2.51 MB)
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Publication date
2023
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Institut für Chemie und Bioanalytik
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01A - Journal article
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Parent work
Chemical Communications
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DOI of the original publication
https://doi.org/10.1039/D3CC01946B
URI
https://irf.fhnw.ch/handle/11654/45473
https://doi.org/10.26041/fhnw-8785
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Volume
59
Issue / Number
62
Pages / Duration
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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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Subject (DDC)
500 - Naturwissenschaften und Mathematik
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1359-7345
1364-548X
0009-241X
Language
English
Created during FHNW affiliation
Yes
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Published
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Peer review of the complete publication
Open access category
Hybrid
License
'https://creativecommons.org/licenses/by/4.0/'
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
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