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
Artificial (transfer) hydrogenases have been developed for organic synthesis, but they rely on precious metals. Native hydrogenases use Earth-abundant metals, but these cannot be applied for organic synthesis due, in part, to their substrate specificity. Herein, we report the design and development of manganese transfer hydrogenases based on the biotin-streptavidin technology. By incorporating bio-mimetic Mn(I) complexes into the binding cavity of streptavidin, and through chemo-genetic optimization, we have obtained artificial enzymes that hydrogenate ketones with nearly quantitative yield and up to 98 % enantiomeric excess (ee). These enzymes exhibit broad substrate scope and high functional-group tolerance. According to QM/MM calculations and X-ray crystallography, the S112Y mutation, combined with the appropriate chemical structure of the Mn cofactor plays a critical role in the reactivity and enantioselectivity of the artificial metalloenzyme (ArMs). Our work highlights the potential of ArMs incorporating base-meal cofactors for enantioselective organic synthesis.
Manganese Transfer Hydrogenases Based on the Biotin-Streptavidin Technology.,Wang W, Tachibana R, Zou Z, Chen D, Zhang X, Lau K, Pojer F, Ward TR, Hu X Angew Chem Int Ed Engl. 2023 Oct 23;62(43):e202311896. doi: , 10.1002/anie.202311896. Epub 2023 Sep 18. PMID:37671593[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang W, Tachibana R, Zou Z, Chen D, Zhang X, Lau K, Pojer F, Ward TR, Hu X. Manganese Transfer Hydrogenases Based on the Biotin-Streptavidin Technology. Angew Chem Int Ed Engl. 2023 Oct 23;62(43):e202311896. PMID:37671593 doi:10.1002/anie.202311896
