Structural highlights
Function
SAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
Publication Abstract from PubMed
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 H2O2 as oxidant, up to approximately 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 (R)-tetralol. X-ray analysis of artificial hydroxylases highlights critical details of the second coordination sphere around the Fe(TAML) cofactor.
Enantioselective Hydroxylation of Benzylic C(sp(3))-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology.,Serrano-Plana J, Rumo C, Rebelein JG, Peterson RL, Barnet M, Ward TR J Am Chem Soc. 2020 Jun 17;142(24):10617-10623. doi: 10.1021/jacs.0c02788. Epub, 2020 Jun 3. PMID:32450689[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Serrano-Plana J, Rumo C, Rebelein JG, Peterson RL, Barnet M, Ward TR. Enantioselective Hydroxylation of Benzylic C(sp(3))-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology. J Am Chem Soc. 2020 Jun 17;142(24):10617-10623. PMID:32450689 doi:10.1021/jacs.0c02788
