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Cover Picture: Photoactivation of an Inhibitor of the 12/15‐Lipoxygenase Pathway (ChemBioChem 7/2006)
Author(s) -
Herre Stephan,
Schadendorf Torsten,
Ivanov Igor,
Herrberger Christian,
Steinle Wencke,
RückBraun Karola,
Preissner Robert,
Kuhn Hartmut
Publication year - 2006
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.200690022
Subject(s) - isomerization , chemistry , moiety , steric effects , stereochemistry , ring (chemistry) , side chain , thiophene , lipoxygenase , catalysis , enzyme , organic chemistry , polymer
The cover picture shows the alignment of the two geometric isomers ( E isomer in blue, Z in turquoise) of 2‐(3‐benzylidene)‐3‐oxo‐2,3‐dihydrobenzo[b]thiophene‐7‐carboxylic acid methyl ester at the active site of rabbit 12/15‐lipoxygenase. In the Z configuration, the benzoyl moiety conflicts with the side chain of the C‐terminal I663, which normally ligates the catalytic non‐heme iron. Light irradiation induces Z ‐to‐ E isomerization, which flips the benzoyl ring over towards I593, the side chain of which limits the depth of the substrate binding pocket. There are no steric constraints for binding of the E isomer. Further details can be found in the article by H. Kuhn et al. on p. 1089 ff.