Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 6522-6525 |
| Number of pages | 4 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 52 |
| Issue number | 25 |
| DOIs | |
| State | Published - 17 Jun 2013 |
Keywords
- biosynthesis
- enzyme catalysis
- iron-sulfur cluster
- metalloproteins
- terpenes
Fingerprint
Dive into the research topics of 'Isoprenoid biosynthesis: Ferraoxetane or allyl anion mechanism for IspH catalysis?'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver