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

Rebelein, Johannes G.; Cotelle, Yoann; Garabedian, Brett; Ward, Thomas R.

doi:10.1021/acscatal.9b01006

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

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Citation

Rebelein, J. G., Cotelle, Y., Garabedian, B., & Ward, T. R. (2019). Chemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase as Host Protein. ACS CATALYSIS, 9(5), 4173-4178. doi:10.1021/acscatal.9b01006.

Cite as: https://hdl.handle.net/21.11116/0000-0008-D636-A

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.