On the 'rebound' mechanism of alkane hydroxylation by cytochrome P450: Electronic structure of the intermediate and the electron transfer character in the rebound step

Michael Filatov, Nathan Harris, Sason Shaik*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

92 Scopus citations

Abstract

Two electromeric forms, a and b (a is the ground state in a solvent) exist for the hydroxo-iron complex 1, an intermediate in the rebound mechanism of alkane hydroxylation by cytochrome P450. Results of density functional and model solvent calculations of various species are in agreement with experimental findings, and imply the role of 1a in the rebound mechanism.

Original languageEnglish
Pages (from-to)3510-3512
Number of pages3
JournalAngewandte Chemie - International Edition
Volume38
Issue number23
DOIs
StatePublished - 3 Dec 1999

Keywords

  • Alkane hydroxylations
  • C-H activation
  • CytoChrome P450
  • Density functional calculations
  • Enzyme catalysis

Fingerprint

Dive into the research topics of 'On the 'rebound' mechanism of alkane hydroxylation by cytochrome P450: Electronic structure of the intermediate and the electron transfer character in the rebound step'. Together they form a unique fingerprint.

Cite this