Polymer Enzyme Conjugates as Chiral Ligands for Sharpless Dihydroxylation of Alkenes in Organic Solvents

• Published in: Chembiochem : a European journal of chemical biology Vol. 16; no. 1; pp. 83 - 90
• Main Authors: Konieczny, Stefan, Leurs, Melanie, Tiller, Joerg C.
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 02-01-2015; WILEY‐VCH Verlag; Wiley Subscription Services, Inc
• Subjects: Alkenes - chemistry; artificial metalloenzymes; asymmetric catalysis; Biocatalysis; Chymotrypsin - chemistry; Enzymes; Fungal Proteins - chemistry; Hydroxylation; Laccase - chemistry; Ligands; Lipase - chemistry; Muramidase - chemistry; organic solvents; Oxazoles - chemistry; Peroxidase - chemistry; polymer enzyme conjugates; Polymers - chemistry; Sharpless dihydroxylation; Solvents; Stereoisomerism; organic solvents; asymmetric catalysis; Sharpless dihydroxylation; polymer enzyme conjugates; artificial metalloenzymes
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.201402339

Conjugates of enzymes and poly(2‐methyloxazoline) were used as organosoluble amphiphilic polymer nanocontainers for dissolving osmate, thereby converting the enzymes into organosoluble artificial metalloenzymes. These were shown to catalyze the dihydroxylation of different alkenes with high enantioselectivity. The highest selectivities, found for osmate complexed with laccase polymer–enzyme conjugates (PECs), even exceed those of classical Sharpless catalysts.
Count Os in: We report organosoluble artificial metalloenzymes, generated from poly(2‐methyl‐oxazoline) enzyme conjugates and osmate as a promising new catalytic system for the dihydroxylation of alkenes in organic media.