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

This publication has 18 references indexed in Scilit:

• THE HAEM‐ACCESSIBILITY IN LEGHAEMOGLOBIN OF LUPINUS LUTEUS AS OBSERVED BY PROTON MAGNETIC RELAXATION
  International Journal of Peptide and Protein Research, 1976
• Cytochrome P450cam and its complexes, Mo¨ssbauer parameters of the heme iron
  Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976
• The haem-environment in horseradish peroxidase as seen by proton magnetic relaxation
  Biochemical and Biophysical Research Communications, 1975
• The magnetic susceptibility of reduced cytochrome P-450cam
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
• The molecular mechanism of the temperature enhancement of proton magnetic relaxation rates in methaemoprotein solutions
  Biophysical Chemistry, 1974
• A gel-electrophoretically homogeneous preparation of cytochrome P-450 from liver microsomes of phenobarbital-pretreated rabbits
  Biochemical and Biophysical Research Communications, 1974
• The role of water in deoxygenated hemoglobin solutions
  Biochemical and Biophysical Research Communications, 1966
• ENZYME-STRUCTURE RELATIONSHIPS IN THE ENDOPLASMIC RETICULUM OF RAT LIVER
  The Journal of cell biology, 1962
• Studies on succinic and DPNH dehydrogenase preparations by paramagnetic resonance (EPR) spectroscopy
  Biochemical and Biophysical Research Communications, 1960
• PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
  Journal of Biological Chemistry, 1951