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Resonance Raman study of the cytochrome P-450 LM2-halothane intermediate complex.

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Hildebrandt,  P.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

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Stier,  A.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

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Stockburger,  M.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Hildebrandt, P., Garda, H., Stier, A., Stockburger, M., & Van Dyke, R. A. (1988). Resonance Raman study of the cytochrome P-450 LM2-halothane intermediate complex. FEBS Letters, 237(1-2), 15-20.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-465F-3
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.