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 journalArticle

138 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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