Highly purified microsomal P-450: the oxyferro intermediate stabilized at low temperature.

[1]  P. Debey,et al.  P450cam: oxygenated complexes stabilized at low temperature. , 1977, Biochemical and biophysical research communications.

[2]  P. Debey,et al.  Sub‐zero temperature studies of microsomal cytochrome P‐450: Interaction of Fe2+ with oxygen , 1977, FEBS letters.

[3]  M. J. Coon,et al.  Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. , 1976, The Journal of biological chemistry.

[4]  M. J. Coon,et al.  Spectral intermediates in the reaction of oxygen with purified liver microsomal cytochrome P-450. , 1976, Biochemical and biophysical research communications.

[5]  C. Larroque,et al.  Practical potentiometric determinations of proton activity in hydro organic solvents at subzero temperatures. , 1976, Analytical biochemistry.

[6]  S. Sligar,et al.  Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam. , 1976, The Journal of biological chemistry.

[7]  F. Travers,et al.  Spectroscopic determinations of enzyme-catalyzed reactions at subzero temperatures. , 1974, Analytical biochemistry.

[8]  B. Griffin,et al.  Pseudomonas putida cytochrome P-450: characterization of an oxygenated form of the hemoprotein. , 1972, Archives of biochemistry and biophysics.

[9]  R. Estabrook,et al.  A new spectral intermediate associated with cytochrome P-450 function in liver microsomes. , 1971, Biochemical and biophysical research communications.