Journal
ACS CATALYSIS
Volume 9, Issue 5, Pages 4173-4178Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.9b01006
Keywords
artificial metalloenzymes; biocatalysis; organometallic chemistry; protein engineering; synthetic biology
Categories
Funding
- Swiss National Science Foundation [200020_182046/1]
- NCCR Molecular Systems Engineering
- ERC
- EMBO [ALTF 194-2017]
- Swiss National Science Foundation (SNF) [200020_182046] Funding Source: Swiss National Science Foundation (SNF)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available