6Y34
Streptavidin wildtype with a biotC5-1 cofactor - an artificial iron hydroxylase
This is a non-PDB format compatible entry.
Summary for 6Y34
| Entry DOI | 10.2210/pdb6y34/pdb |
| Descriptor | Streptavidin, biotC5-1 cofactor, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | artificial metalloenzyme, iron hydroxylase, biotin-binding protein, oxidoreductase |
| Biological source | Streptomyces avidinii |
| Total number of polymer chains | 1 |
| Total formula weight | 17342.71 |
| Authors | Serrano-Plana, J.,Rumo, C.,Rebelein, J.G.,Peterson, R.L.,Barnet, M.,Ward, T.R. (deposition date: 2020-02-17, release date: 2020-07-01, Last modification date: 2024-01-24) |
| Primary citation | Serrano-Plana, J.,Rumo, C.,Rebelein, J.G.,Peterson, R.L.,Barnet, M.,Ward, T.R. Enantioselective Hydroxylation of Benzylic C(sp3)-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology. J.Am.Chem.Soc., 142:10617-10623, 2020 Cited by PubMed Abstract: The selective hydroxylation of C-H bonds is of great interest to the synthetic community. Both homogeneous catalysts and enzymes offer complementary means to tackle this challenge. Herein, we show that biotinylated Fe(TAML)-complexes (TAML = Tetra Amido Macrocyclic Ligand) can be used as cofactors for incorporation into streptavidin to assemble artificial hydroxylases. Chemo-genetic optimization of both cofactor and streptavidin allowed optimizing the performance of the hydroxylase. Using HO as oxidant, up to ∼300 turnovers for the oxidation of benzylic C-H bonds were obtained. Upgrading the ee was achieved by kinetic resolution of the resulting benzylic alcohol to afford up to >98% ee for ()-tetralol. X-ray analysis of artificial hydroxylases highlights critical details of the second coordination sphere around the Fe(TAML) cofactor. PubMed: 32450689DOI: 10.1021/jacs.0c02788 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.307 Å) |
Structure validation
Download full validation report
