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 metalloenzymes (ArMs) enable the integration of abiotic cofactors within a native protein scaffold, allowing for non-natural catalytic activities. Previous ArMs, however, have primarily relied on single cofactor systems, limiting them to only one catalytic function. Here we present an approach to construct ArMs embedding two catalytic cofactors based on the biotin-streptavidin technology. By incorporating multiple catalytic cofactors into the four binding sites of streptavidin, we engineered programmable ArMs for tandem abiotic transformations including an enantioselective formal C-H hydroxylation and a photooxidation-Michael addition. This work thus outlines a promising strategy for the development of ArMs embedding multiple cofactors.
Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations.,Wang W, Tachibana R, Zhang K, Lau K, Pojer F, Ward TR, Hu X Angew Chem Int Ed Engl. 2025 Jan 6:e202422783. doi: 10.1002/anie.202422783. PMID:39760306[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang W, Tachibana R, Zhang K, Lau K, Pojer F, Ward TR, Hu X. Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations. Angew Chem Int Ed Engl. 2025 Jan 6:e202422783. PMID:39760306 doi:10.1002/anie.202422783
