Studies of the unique nature of the cytochrome P-450 active site. Electron spin resonance spectroscopy as a probe of the hemin iron of cytochrome P-450: the influence of buffer composition, alcohols, and nitrogenous ligands

Arch Biochem Biophys. 1977 Sep;183(1):317-27. doi: 10.1016/0003-9861(77)90445-3.
No abstract available

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alkanesulfonates
  • Animals
  • Binding Sites
  • Buffers*
  • Camphor / metabolism
  • Cytochrome P-450 Enzyme System / metabolism*
  • Electron Spin Resonance Spectroscopy
  • Heme* / analogs & derivatives
  • Hemin*
  • Male
  • Membranes
  • Methanol*
  • Methylcholanthrene / pharmacology
  • Metyrapone*
  • Microsomes, Liver
  • Morpholines
  • Phenobarbital / pharmacology
  • Pseudomonas
  • Rats

Substances

  • Alkanesulfonates
  • Buffers
  • Morpholines
  • Heme
  • Methylcholanthrene
  • Hemin
  • Camphor
  • Cytochrome P-450 Enzyme System
  • Methanol
  • Phenobarbital
  • Metyrapone