New synthetic models of cytochrome P450: How different are they from the natural species?

Sebastian Kozuch, Tycho Leifels, Dominik Meyer, Laura Sbaragli, Sason Shaik, Wolf D. Woggon

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Soluble and matrix-bound P450 enzyme models have been synthesized carrying a SO3- ligand coordinating to iron. These complexes display features very similar to cofactors of enzymes such as P450cam with respect to electrochemistry and UV/Vis spectroscopy. Further they catalyze epoxidation reactions with turnover numbers up to 1800. DFT calculations revealed that the coordination of SO3- to Fe(III) produces an active species that displays allylic hydroxylation and epoxidation reactivity patterns that are nearly indistinguishable from those calculated for the natural active species of the enzyme cytochrome P450.

Original languageEnglish
Pages (from-to)675-684
Number of pages10
JournalSynlett
Issue number4
DOIs
StatePublished - 4 Mar 2005
Externally publishedYes

Keywords

  • Catalysis
  • DFT calculations
  • Enzyme models
  • Hemethiolate proteins
  • Iron porphyrins

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