TY - JOUR
T1 - Sodium periodate, sodium chlorite, organic hydroperoxides, and H2O2 as hydroxylating agents in steroid hydroxylation reactions catalyzed by partially purified cytochrome P-450
AU - Hrycay, Eugene G.
AU - Gustafsson, Jan åke
AU - Ingelman-Sundberg, Magnus
AU - Ernster, Lars
N1 - Funding Information:
Acknowledgments: We thank Mrs. G. Elfstr6m, Miss G. Bj6rk, and Miss I. Johansson for skillful technical assistance and thank the Canadian Medical Research Council, the Swedish Medical Research Council (grant no. 03X-2819), and NIH (grant no. NO1 CP33363) for support.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1975/9/2
Y1 - 1975/9/2
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(75)80315-9
DO - 10.1016/S0006-291X(75)80315-9
M3 - Article
C2 - 240357
AN - SCOPUS:0016837241
VL - 66
SP - 209
EP - 216
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -