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Chemistry. 2018 Jul 25;24(42):10859-10867. doi: 10.1002/chem.201802185. Epub 2018 Jun 27.

Multicore Artificial Metalloenzymes Derived from Acylated Proteins as Catalysts for the Enantioselective Dihydroxylation and Epoxidation of Styrene Derivatives.

Author information

1
Chair of Biomaterials and Polymer Science, Department of Biochemical and Chemical Engineering, TU Dortmund, Emil-Figge-Str. 66, 44227, Dortmund, Germany.

Abstract

Artificial metalloenzymes (AME's) are an interesting class of selective catalysts, where the chiral environment of proteins is used as chiral ligand for a catalytic metal. Commonly, the active site of an enzyme is modified with a catalytically active metal. Here we present an approach, where the commercial proteins lysozyme (LYS) and bovine serum albumin (BSA) can be converted into highly active and enantioselective AME's. This is achieved by acylation of the proteins primary amino groups, which affords the metal salts in the core of the protein. A series of differently acylated LYS and BSA were reacted with K2 OsO2 (OH)4 , RuCl3 , and Ti(OMe)4 , respectively, and the conjugates were tested for their catalytic activity in dihydroxylation and epoxidation of styrene and its derivatives. The best suited system for dihydroxylation is fully acetylated LYS conjugated with K2 OsO2 (OH)4 , which converts styrene to 1,2-phenylethanediol with an enantioselectivity of 95 % ee (S). BSA fully acylated with hexanoic acid and conjugated with three moles RuCl3 per mole protein shows the highest ee values for the conversion of styrene to the respective epoxide with enenatioselectivities of over 80 % ee (R), a TON of more than 2500 and a yield of up to 78 % within 24 h at 40 °C. LYS has two favored selective binding sites for the metal catalyst and BSA has even three. The AME's with titanate in the active center invert the enantioselectivity of styrene epoxidation.

KEYWORDS:

asymmetric catalysis; asymmetric dihydroxylation; asymmetric epoxidation; metalloenzymes; proteins

PMID:
29808506
DOI:
10.1002/chem.201802185
[Indexed for MEDLINE]

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