Haem accessibility in cytochrome P-450 from rabbit liver. A proton magnetic relaxation study by stereochemical probes

H. Rein, S. Maricic, G. R. Jänig, S. Vuk-Pavlovic, B. Benko, O. Ristau, K. Ruckpaul

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Abstract

Cytochrome P-450 was solubilized from phenobarbital induced rabbit liver and purified by affinity chromatography. The longitudinal proton magnetic relaxation rates of this ferric, low-spin sample (as confirmed by ESR) in 20% glycerol aqueous solution are very large compared with low-spin methaemoglobin and myoglobin derivatives. Similarly high rates were measured in a deuterated solution using the aliphatic protons of glycerol as stereochemical markers, which strongly suggests that the haem iron in cytochrome P-450 is much more accessible to the solvent than in haemoglobin or myoglobin. Type I substrate (Spasman®) produced small but significant increases in NMR rates both in the H2O and in the 2H2O solution, while binding of aniline (Type II substrate) doubled the rates.

Original languageEnglish (US)
Pages (from-to)325-330
Number of pages6
JournalBBA - Protein Structure
Volume446
Issue number1
DOIs
StatePublished - Sep 28 1976

ASJC Scopus subject areas

  • Medicine(all)

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    Rein, H., Maricic, S., Jänig, G. R., Vuk-Pavlovic, S., Benko, B., Ristau, O., & Ruckpaul, K. (1976). Haem accessibility in cytochrome P-450 from rabbit liver. A proton magnetic relaxation study by stereochemical probes. BBA - Protein Structure, 446(1), 325-330. https://doi.org/10.1016/0005-2795(76)90123-9