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
Introduction of a biotinylated monophosphine palladium complex within streptavidin affords an enantioselective artificial Suzukiase. Site-directed mutagenesis allowed the optimization of the activity and the enantioselectivity of this artificial metalloenzyme. A variety of atropisomeric biaryls were produced in good yields and up to 90% ee. The hybrid catalyst described herein shows comparable TOF to the previous aqueous-asymmetric Suzuki catalysts, and excellent stability under the reaction conditions to realize higher TON through longer reaction time.
An enantioselective artificial Suzukiase based on the biotin-streptavidin technology.,Chatterjee A, Mallin H, Klehr J, Vallapurackal J, Finke AD, Vera L, Marsh M, Ward TR Chem Sci. 2016 Jan 1;7(1):673-677. doi: 10.1039/c5sc03116h. Epub 2015 Oct 19. PMID:29896353[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chatterjee A, Mallin H, Klehr J, Vallapurackal J, Finke AD, Vera L, Marsh M, Ward TR. An enantioselective artificial Suzukiase based on the biotin-streptavidin technology. Chem Sci. 2016 Jan 1;7(1):673-677. doi: 10.1039/c5sc03116h. Epub 2015 Oct 19. PMID:29896353 doi:http://dx.doi.org/10.1039/c5sc03116h
