Mechanism of aliphatic hydroxylation. Tetralin hydroperoxide as an intermediate in the hydroxylation of tetralin in rat-liver homogenate.

doi:10.1016/0304-4165(68)90016-0

Paper

Mechanism of aliphatic hydroxylation. Tetralin hydroperoxide as an intermediate in the hydroxylation of tetralin in rat-liver homogenate.

Published Dec 23, 1968 · C. Chen, C. C. Lin

Biochimica et biophysica acta

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16

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Abstract

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In Vitro Study

Study Snapshot

Tetralin hydroperoxide acts as an intermediate in the hydroxylation of tetralin to tetralol in rat-liver homogenate, eliminating the possibility of mono-atomic oxygen species as a reactant.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Mechanism of aliphatic hydroxylation. Tetralin hydroperoxide as an intermediate in the hydroxylation of tetralin in rat-liver homogenate.

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References

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Rabbit muscle aldolase can be reactivated by mercaptoethanol, cyanide, or borohydride, but not by metal ions.

Hydroxylation of steroids at carbon 21.

C-21 hydroxylation of steroids by adrenal tissue preparations is an essential step in the synthesis of steroid hormones by this gland.

The mechanism of the oxidation of unsaturated fatty acids catalyzed by hematin compounds.

Linoleate oxidation is initiated by direct reaction of linoleate peroxide with hematin catalysts, with propagation likely similar to autocatalytic linoleate oxidation.

ASCORBIC ACID IN AROMATIC HYDROXYLATION I. A MODEL SYSTEM FOR AROMATIC HYDROXYLATION* BY SIDNEY UDENFRIEND, CARROLL T. CLARK, JULIUS AXELROD, AND BERNARD B. BRODIE

Ascorbic acid plays a crucial role in the hydroxylation of aromatic compounds in the animal body, leading to phenolic products with a variety of pathways still unclear.

The inhibitory effects in vitro of phenothiazines and other drugs on lipid-peroxidation systems in rat liver microsomes, and their relationship to the liver necrosis produced by carbon tetrachloride.

Promethazine effectively inhibits lipid peroxidation in rat liver microsomes, potentially protecting against liver necrosis caused by carbon tetrachloride.

Citations

Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P-450.

Purified liver microsomal cytochrome P-450 catalyzes hydroperoxide-dependent hydroxylation of various substrates, with a peroxidase-like mechanism for its action.

Sterol metabolism: XXXVII. On the oxidation of cholesterol by dioxygenases

Plant and mammalian dioxygenases oxidize cholesterol, mimicking radiation-induced free radical oxidation by molecular oxygen, without electronically excited molecular oxygen.

Hydroperoxide dependent O-dealkylation reactions catalyzed by liver microsomal cytochrome P450.

Cytochrome P450 catalyzes the O-dealkylation of methoxy and ethoxy compounds in hepatic microsomes, with higher substrate specificity than NADPH-dependent reactions.

Hydroperoxide peroxidase activity in liver microsomes.

NADH- and NADPH-dependent peroxidase activity in liver microsomes may be mediated by separate components of the microsomal electron transport chain, distinct from but closely interacting with cytochrome P 450.

Cytochrome P-450 as a microsomal peroxidase in steroid hydroperoxide reduction.

Cytochrome P-450 plays a crucial role in steroid hydroperoxide reduction, converting 17-hydroperoxide derivatives of progesterone, pregnenolone, and allopregnanolone into 17-hydroxy derivatives.