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Chemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase as Host Protein

Rebelein, Johannes G. and Cotelle, Yoann and Garabedian, Brett and Ward, Thomas R.. (2019) Chemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase as Host Protein. ACS Catalysis, 9 (5). pp. 4173-4178.

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Official URL: https://edoc.unibas.ch/70593/

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Abstract

Artificial metalloenzymes combine a synthetic metallocofactor with a protein scaffold and can catalyze abiotic reactions in vivo. Herein, we report on our efforts to valorize human carbonic anhydrase II as a scaffold for whole-cell transfer hydrogenation. Two platforms were tested: periplasmic compartmentalization and surface display in Escherichia coli. A chemical optimization of an IrCp* cofactor was performed. This led to 90 turnovers in the cell, affording a 69-fold increase in periplasmic product formation over the previously reported, sulfonamide-bearing IrCp* cofactor. These findings highlight the versatility of carbonic anhydrase as a promising scaffold for whole-cell catalysis with artificial metalloenzymes.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Ward, Thomas R. R. and Rebelein, Johannes Georg and Cotelle, Yoann and Garabedian, Brett
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:ACS Publications
ISSN:0140-0568
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
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Last Modified:04 Jul 2019 14:29
Deposited On:23 May 2019 12:46

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