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Resonance Raman study of the cytochrome P-450 LM2-halothane intermediate complex
P Hildebrandt1, H Garda, A Stier
1Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, Göttingen, FRG.
FEBS Letters
|September 12, 1988
Abstract:
Resonance Raman (RR) and absorption spectroscopic studies of purified rabbit liver cytochromes P-450 show that the form 2 isomer (LM2) but not the form 4 isomer (LM4) forms a long-lived complex with halothane after dithionite reduction, absorbing light at 470 nm, in which ferric 6-coordinated heme iron in the low-spin configuration is liganded to 2-chloro-1,1-difluoroethylene. The RR data exclude the possibility that the CF3CHCl- carbanion is a ligand and are consistent with the involvement of an active-site pocket in the cytochrome P-450 polypeptide.