Download MendeleyChemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase as Host Protein.
Rebelein, J.G., Cotelle, Y., Garabedian, B., Ward, T.R.(2019) ACS Catal 9: 4173-4178
- PubMed: 31080690
- DOI: https://doi.org/10.1021/acscatal.9b01006
- Primary Citation of Related Structures:
6QFU, 6QFV, 6QFW, 6QFX - PubMed 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.
Organizational Affiliation:
Department of Chemistry, University of Basel, BPR 1096, Mattenstrasse 24a, 4058 Basel, Switzerland.
