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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-465F-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-4661-C
Genre: Journal Article

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Hildebrandt, P.1, Author              
Garda, H., Author
Stier, A.1, Author              
Stockburger, M.1, Author              
Van Dyke, R. A., Author
Affiliations:
1Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society, ou_578624              

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 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.

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Language(s): eng - English
 Dates: 1988-09-12
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: CoNE: 1016/0014-5793(88)80162-5
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 237 (1-2) Sequence Number: - Start / End Page: 15 - 20 Identifier: -