Reactive iron porphyrin derivatives related to the catalytic cycles of cytochrome P-450 and peroxidase. Studies of the mechanism of oxygen activation

This publication has 17 references indexed in Scilit:

• Evidence for a homolytic mechanism of peroxide oxygen–oxygen bond cleavage during substrate hydroxylation by cytochrome P-450.
  Journal of Biological Chemistry, 1980
• Models for the active site of oxygen-binding hemoproteins. Dioxygen binding properties and the structures of (2-methylimidazole)-meso-tetra(.alpha.,.alpha.,.alpha.,.alpha.-o-pivalamidophenyl)porphyrinatoiron(II)-ethanol and its dioxygen adduct
  Journal of the American Chemical Society, 1980
• Chemical mechanisms for cytochrome P-450 hydroxylation: evidence for acylation of heme-bound dioxygen.
  Proceedings of the National Academy of Sciences, 1980
• The missing heme spin state and a model for cytochrome c'. The mixed S = 3/2, 5/2 intermediate spin ferric porphyrin: perchlorato(meso-tetraphenylporphinato)iron(III)
  Journal of the American Chemical Society, 1979
• Iodosylbenzene derivatives as oxygen donors in cytochrome P-450 catalyzed steroid hydroxylations
  Biochemistry, 1979
• Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P-450
  Archives of Biochemistry and Biophysics, 1976
• Cytochrome P450 as an oxene transferase
  Biochemical and Biophysical Research Communications, 1976
• Sodium periodate, sodium chlorite, organic hydroperoxides, and H2O2 as hydroxylating agents in steroid hydroxylation reactions catalyzed by partially purified cytochrome P-450
  Biochemical and Biophysical Research Communications, 1975
• PHARMACOLOGICAL IMPLICATIONS OF MICROSOMAL ENZYME INDUCTION
  1967
• THE PROPERTIES OF THE ENZYME-SUBSTRATE COMPOUNDS OF PEROXIDASE AND PEROXIDES .1. THE SPECTRA OF THE PRIMARY AND SECONDARY COMPLEXES
  1949