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Cover Picture: Enzymatic Fluorination in Streptomyces cattleya Takes Place with an Inversion of Configuration Consistent with an S N 2 Reaction Mechanism (ChemBioChem 5/2004)
Author(s) -
Cadicamo Cosimo D.,
Courtieu Jacques,
Deng Hai,
Meddour Abdelkrim,
O'Hagan David
Publication year - 2004
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.200490021
Subject(s) - chemistry , enantiomer , absolute configuration , stereochemistry , streptomyces , chirality (physics) , biocatalysis , fluoride , methyl group , group (periodic table) , reaction mechanism , computational chemistry , organic chemistry , catalysis , inorganic chemistry , physics , genetics , nambu–jona lasinio model , chiral symmetry breaking , quantum mechanics , bacteria , biology , quark
The cover picture shows a mechanism of the fluorination enzyme from Streptomyces cattleya whereby a fluoride ion mediates a nucleophilic substitution reaction on S ‐adenosyl‐ L ‐methionine (SAM). This conclusion is drawn after exploring the enzyme reaction with deuterium‐labelled (5′ S )‐[5′‐ 2 H 1 ]‐SAM to generate a product with a chiral fluoromethyl group. Enantiomeric assay for the chiral fluoromethyl group by 2 H NMR in a chiral liquid‐crystalline medium (the Courtieu method) allowed evaluation of the absolute configuration of the resultant chiral fluoromethyl group. More details on this study by A. Meddour, D. O'Hagan et al. are described on p. 685 ff.