Sodium periodate, sodium chlorite, organic hydroperoxides, and H2O2 as hydroxylating agents in steroid hydroxylation reactions catalyzed by partially purified cytochrome P-450

Eugene G. Hrycay, Jan åke Gustafsson, Magnus Ingelman-Sundberg, Lars Ernster

Research output: Contribution to journalArticlepeer-review

140 Scopus citations

Abstract

The mechanism of androstenedione hydroxylation has been examined by employing NADPH, NaIO4, NaCLO2, H2O2, and organic hydroperoxides as hydroxylating agents and partially purified cytochrome P-450, prepared from phenobarbital-induced rat liver microsomes, as the catalyst. The NADPH-supported hydroxylation also required NADPH-cytochrome P-450 reductase. Androstenedione was hydroxylated in the 6β-, 7α-, and 16α-positions to varying degrees depending on the hydroxylating agent. NaIO4 was the most effective agent followed by cumene hydroperoxide, NADPH, Linoleic acid hydroperoxide, NaCLO2, t-butyl hydroperoxide, and H2O2. It was suggested that the ferryl ion (compound I) of cytochrome P-450 is the common "activated oxygen" species in these hydroxylations.

Original languageEnglish (US)
Pages (from-to)209-216
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume66
Issue number1
DOIs
StatePublished - Sep 2 1975

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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