NADH‐Dependent Aryl Hydrocarbon Hydroxylase in Rat Liver Mitochondrial Outer Membrane
- 1 July 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 66 (2) , 293-307
- https://doi.org/10.1111/j.1432-1033.1976.tb10519.x
Abstract
NADH-dependent 3,4-benzpyrene hydroxylase activity was detected in the purified mitochondrial outer membrane fraction from the livers of rats treated with 3-methylcholanthrene. The specific activity in the outer membrane fraction is nearly equal to that of microsomes, a level too high to be accounted for only by the microsomal contamination. The NADPH-dependent 3,4-benzpyrene hydroxylase activity in the outer membrane fraction is about 50% of that of microsomes. The ratio of the specific activity of NADPH to NADH-dependent 3,4-benzpyrene hydroxylase in microsomal fraction was about 3.5, while that of the outer membrane fraction was about 1.5. NADH-dependent 3,4-benzpyrene hydroxylase activity in the mitochondrial outer membrane from control rat liver was cyanide-insensitive, while that in microsomes was cyanide-sensitive. These results suggest that aryl hydrocarbon hydroxylase activity, which uses NADH almost as efficiently as NADPH, is present in the mitochondrial outer membrane fraction. The hydroxylase system is composed of cyanide-insensitive cytochrome P-450 and is inducible markedly by 3-methylcholanthrene treatment. The probable electron transfer pathways in the mitochondrial outer membrane cytochrome P-450 oxidase system are discussed.This publication has 57 references indexed in Scilit:
- A microsomal iron-sulfur center in rat liverBiochemical and Biophysical Research Communications, 1975
- Hydroperoxide catalyzed liver microsomal aromatic hydroxylation reactions involving cytochrome P-450Biochemical and Biophysical Research Communications, 1974
- Liver microsomal electron transport systems: II. The involvement of cytochrome b5 in the NADH-dependent hydroxylation of 3,4-benzpyrene by a reconstituted cytochrome P-448-containing systemBiochemical and Biophysical Research Communications, 1974
- The possible involvement of cytochrome b5 in the oxidation of lauric acid by microsomes from kidney cortex and liver of ratsLife Sciences, 1974
- Alteration in the microsomal hemoprotein and the kinetics of 3,4-benzypyrene hydroxylase induced by 3-methylcholanthrene: Time course study and effects of puromycinLife Sciences, 1971
- Cytochrome b5 and co-binding cytochromes in the Golgi membranes of mammalian liversBiochemical and Biophysical Research Communications, 1970
- Enzyme localization in the inner and outer mitochondrial membranesBiochemical and Biophysical Research Communications, 1968
- Differences in the kinetics of benzpyrene hydroxylation by hepatic drug-metabolizing enzymes from phenobarbital and 3-methylcholanthrene-treated ratsBiochemical and Biophysical Research Communications, 1968
- A non-heme iron protein from pig testis and its substitution for adrenal non-heme iron protein (adrenodoxin) in steroid 11β-hydroxylationBiochemical and Biophysical Research Communications, 1967
- Study of the adrenal non-heme iron protein (adrenodoxin) by electron spin resonanceBiochemical and Biophysical Research Communications, 1966