6QFU

Human carbonic anhydrase II with bound IrCp* complex (cofactor 7) to generate an artificial transfer hydrogenase (ATHase)

Summary for 6QFU

• Entry DOI: 10.2210/pdb6qfu/pdb
• Descriptor: Carbonic anhydrase 2, 4-[2-(9-chloranyl-2',3',4',5',6'-pentamethyl-4-oxidanyl-7-oxidanylidene-spiro[1$l^{4},8-diaza-9$l^{8}-iridabicyclo[4.3.0]nona-1(6),2,4-triene-9,1'-1$l^{8}-iridapentacyclo[2.2.0.0^{1,3}.0^{1,5}.0^{2,6}]hexane]-8-yl)ethyl]benzenesulfonamide, ZINC ION, ... (5 entities in total)
• Functional Keywords: artificial transfer hydrogenase, bound ircp* complex, zinc binding protein, human carbonic anhydrase ii, oxidoreductase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 30117.77

Authors

Rebelein, J.G. (deposition date: 2019-01-10, release date: 2019-04-17, Last modification date: 2024-01-24)

Primary citation

Rebelein, J.G.,Cotelle, Y.,Garabedian, B.,Ward, T.R.
Chemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase as Host Protein.
Acs Catalysis, 9:4173-4178, 2019

PubMed Abstract: Artificial metalloenzymes combine a synthetic metallocofactor with a protein scaffold and can catalyze abiotic reactions . 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 . 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.

PubMed: 31080690
DOI: 10.1021/acscatal.9b01006

Experimental method

X-RAY DIFFRACTION (1.8 Å)