Hildebrandt P, Garda H, Stier A, Stockburger M, Van Dyke R A
Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, Göttingen, FRG.
FEBS Lett. 1988 Sep 12;237(1-2):15-20. doi: 10.1016/0014-5793(88)80162-5.
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.
