English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

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

MPS-Authors
/persons/resource/persons15229

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

/persons/resource/persons15875

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

/persons/resource/persons15876

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

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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: https://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.