Isoprenoid biosynthesis: Ferraoxetane or allyl anion mechanism for IspH catalysis?

Jikun Li, Ke Wang, Tatyana I. Smirnova, Rahul L. Khade, Yong Zhang, Eric Oldfield

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

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 languageEnglish
Pages (from-to)6522-6525
Number of pages4
JournalAngewandte Chemie - International Edition
Volume52
Issue number25
DOIs
StatePublished - 17 Jun 2013

Keywords

  • biosynthesis
  • enzyme catalysis
  • iron-sulfur cluster
  • metalloproteins
  • terpenes

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