Resonance Raman study of the cytochrome P-450 LM2-halothane intermediate complex.
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.
Hildebrandt
P
P
Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, Göttingen, FRG.
Garda
H
H
Stier
A
A
Stockburger
M
M
Van Dyke
R A
RA
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006221:Halothane / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman / Q000379:methods
D007527:Isoenzymes; D003577:Cytochrome P-450 Enzyme System; D006221:Halothane