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Biosynthesis of Isoprene Units: Mössbauer Spectroscopy of Substrate and Inhibitor Binding to the [4Fe‐4S] Cluster of the LytB/IspH Enzyme
Author(s) -
AhrensBotzong Annegret,
Janthawornpong Karnjapan,
Wolny Juliusz A.,
Tambou Erasmienne Ngouamegne,
Rohmer Michel,
Krasutsky Sergiy,
Poulter C. Dale,
Schünemann Volker,
Seemann Myriam
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104562
Subject(s) - substrate (aquarium) , isoprene , chemistry , enzyme , stereochemistry , cluster (spacecraft) , biochemistry , organic chemistry , computer science , biology , ecology , copolymer , programming language , polymer
A fascinating cube : LytB, an enzyme containing a [4Fe‐4S] cluster, catalyzes the last step of the methylerythritol phosphate pathway, a target for antibacterial and antiparasitic drugs. Field‐dependent Mössbauer spectroscopy showed that the unique fourth iron atom of the [4Fe‐4S] cluster coordinates to the hydroxy group of the substrate (see picture) and to the amino and thiol moieties of two potent inhibitor substrate analogues.