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Cover Picture: Catalytic Promiscuity of Halohydrin Dehalogenase and its Application in Enantioselective Epoxide Ring Opening (ChemBioChem 7/2008)
Author(s) -
HasnaouiDijoux Ghannia,
Majerić Elenkov Maja,
Lutje Spelberg Jeffrey H.,
Hauer Bernhard,
Janssen Dick B.
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200890021
Subject(s) - enantioselective synthesis , chemistry , biocatalysis , dehalogenase , epoxide hydrolase , stereochemistry , combinatorial chemistry , ring (chemistry) , nucleophile , substrate (aquarium) , enzyme , catalysis , organic chemistry , biology , reaction mechanism , ecology , microsome
The cover picture shows a close‐up of the promiscuous halide binding site of halohydrin dehalogenase, an enzyme that catalyzes enantioselective epoxide ring opening with a diversity of anionic nucleophiles. Also shown are conversions that give good yields of building blocks for a range of useful, highly enantioenriched, chiral compounds, including cyanoalcohols, nitroalcohols, and oxazolidinones. These have potential applications in agrochemicals, pharmaceuticals, and polymer chemistry. In the background, recombinant dehalogenase‐producing E. coli colonies appear violet on an eosin–methylene blue indicator plate when exposed to a chloroalcohol substrate. For more information, see the communication by D. B. Janssen et al. on p. 1048 ff. of this issue.