TY - JOUR
T1 - Isoprenoid biosynthesis
T2 - Ferraoxetane or allyl anion mechanism for IspH catalysis?
AU - Li, Jikun
AU - Wang, Ke
AU - Smirnova, Tatyana I.
AU - Khade, Rahul L.
AU - Zhang, Yong
AU - Oldfield, Eric
PY - 2013/6/17
Y1 - 2013/6/17
N2 - 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.
AB - 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.
KW - biosynthesis
KW - enzyme catalysis
KW - iron-sulfur cluster
KW - metalloproteins
KW - terpenes
UR - http://www.scopus.com/inward/record.url?scp=84878923624&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84878923624&partnerID=8YFLogxK
U2 - 10.1002/anie.201302343
DO - 10.1002/anie.201302343
M3 - Article
C2 - 23649534
AN - SCOPUS:84878923624
SN - 1433-7851
VL - 52
SP - 6522
EP - 6525
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 25
ER -