Two-state reactivity in the rebound step of alkane hydroxylation by cytochrome P-450: Origins of free radicals with finite lifetimes

Nathan Harris, Shimrit Cohen, Michael Filatov, François Ogliaro, Sason Shaik*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

100 Scopus citations

Abstract

The model rebound step of alkane hydroxylation exhibits a low-spin (LS) rebound with no barrier, but shows a barrier for the high-spin process (HS). Free radicals are expected primarily in the high-spin rebound. Data from radical clock experiments are examined in terms of this two-state scenario.

Original languageEnglish
Pages (from-to)2003-2007
Number of pages5
JournalAngewandte Chemie - International Edition
Volume39
Issue number11
DOIs
StatePublished - 2 Jun 2000

Keywords

  • Density functional calculations center dot enzyme catalysis
  • Hydroxylations
  • Oxygenases
  • Radicals

Fingerprint

Dive into the research topics of 'Two-state reactivity in the rebound step of alkane hydroxylation by cytochrome P-450: Origins of free radicals with finite lifetimes'. Together they form a unique fingerprint.

Cite this