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 Cited by 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: 31080690DOI: 10.1021/acscatal.9b01006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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