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

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 enantios...

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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
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Abstract 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.
AbstractList 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.
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.
Author Tiller, Joerg C.
Konieczny, Stefan
Leurs, Melanie
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  givenname: Melanie
  surname: Leurs
  fullname: Leurs, Melanie
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  givenname: Joerg C.
  surname: Tiller
  fullname: Tiller, Joerg C.
  email: joerg.tiller@tu-dortmund.de
  organization: Chair of Biomaterials and Polymer Science, Department of Biochemical and Chemical Engineering, TU Dortmund, Emil-Figge-Strasse 66, 44227 Dortmund (Germany)
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Issue 1
Keywords organic solvents
asymmetric catalysis
Sharpless dihydroxylation
polymer enzyme conjugates
artificial metalloenzymes
Language English
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Snippet Conjugates of enzymes and poly(2‐methyloxazoline) were used as organosoluble amphiphilic polymer nanocontainers for dissolving osmate, thereby converting the...
Conjugates of enzymes and poly(2-methyloxazoline) were used as organosoluble amphiphilic polymer nanocontainers for dissolving osmate, thereby converting the...
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StartPage 83
SubjectTerms 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
Title Polymer Enzyme Conjugates as Chiral Ligands for Sharpless Dihydroxylation of Alkenes in Organic Solvents
URI https://api.istex.fr/ark:/67375/WNG-TJK0DX97-3/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fcbic.201402339
https://www.ncbi.nlm.nih.gov/pubmed/25421303
https://www.proquest.com/docview/1639257957
https://search.proquest.com/docview/1640327606
Volume 16
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