Premium
Isoprenoid Biosynthesis: Ferraoxetane or Allyl Anion Mechanism for IspH Catalysis?
Author(s) -
Li Jikun,
Wang Ke,
Smirnova Tatyana I.,
Khade Rahul L.,
Zhang Yong,
Oldfield Eric
Publication year - 2013
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.201302343
Subject(s) - mechanism (biology) , chemistry , biosynthesis , stereochemistry , catalysis , enzyme , computer science , service (business) , combinatorial chemistry , world wide web , information retrieval , biochemistry , computational biology , biology , philosophy , business , epistemology , marketing
The catalytic mechanism of the enzyme IspH, involved in formation of isopentenyl diphosphate and dimethylallyl diphosphate, was investigated by using HYSCORE spectroscopy combined with DFT. The results indicate the formation of an allyl anion bound to a HiPIP‐like oxidized 4Fe–4S cluster, rather than formation of a cyclic, ferraoxetane intermediate, as has been proposed elsewhere.