Aromatic hydroxylation of acetanilide and aniline by hemin2̄thiolester complex as a cytochrome P-450 model

1983 ◽  
Vol 80 ◽  
pp. 7-12 ◽  
Author(s):  
Hiromu Sakurai ◽  
Etsuji Hatayama ◽  
Mikio Nishida
Keyword(s):  
Aromatic Hydroxylation ◽  
Cytochrome P 450

Cytochrome P-450 model reaction: effects of substitution on the rate of aromatic hydroxylation

2000 ◽  
Vol 04 (03) ◽  
pp. 285-291 ◽  
Author(s):  
NASSER SAFARI ◽  
FARZAD BAHADORAN ◽  
MOHAMMAD REZA HOSEINZADEH ◽  
REZA GHIASI
Keyword(s):  
Relative Rate ◽  
Kinetic Method ◽  
Oxidation Reactions ◽  
Aromatic Rings ◽  
Aromatic Hydroxylation ◽  
Catalysed Oxidation ◽  
Epoxidation Of Alkenes ◽  
Cytochrome P 450 ◽  
Related Compounds ◽  
Electron Withdrawing Substituents

The study of haemin-catalysed oxidation reactions was extended to substituted aromatic rings. Both electron-donating and electron-withdrawing substituents on aromatic rings act as para- and meta-directing agents in the presence of tetrakis(2,6-dichlorophenyl)porphyrin iron(III) chloride as catalyst and m-chloroperbenzoic acid as oxidant. A new kinetic method for measuring relative rates of epoxidation of alkenes and related compounds has been developed; while steric hindrance results in decreasing the rate of hydroxylation, electron-rich and electron-withdrawing substituents were found to increase the rate of hydroxylation. A linear relationship between the logarithm of the relative rate of hydroxylation and σ Hammet is obtained, although electron-donating and electron-withdrawing substituents fit separate lines. Addition of pyridine to haemin was shown to increase the yield of epoxidation but decrease the yield of aromatic hydroxylation.

Isotopically labeled chlorobenzenes as probes for the mechanism of cytochrome P-450 catalyzed aromatic hydroxylation

Biochemistry ◽  
1989 ◽  
Vol 28 (23) ◽  
pp. 9019-9027 ◽  
Author(s):  
Kenneth R. Korzekwa ◽  
David C. Swinney ◽  
William F. Trager
Keyword(s):  
Aromatic Hydroxylation ◽  
Cytochrome P 450

scholarly journals Contribution of cytochromes and proteins to the effect of ascorbic acid on artificial and microsomal hydroxylation systems containing oxygen and hydrogen peroxide

1978 ◽  
Vol 170 (3) ◽  
pp. 693-698 ◽  
Author(s):  
J Chrastil ◽  
J T Wilson
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Free Radical ◽  
Cytochrome C ◽  
Rat Liver ◽  
Oxidative Demethylation ◽  
Aromatic Hydroxylation ◽  
Microsomal Hydroxylation ◽  
Cytochrome P 450

Hydroxylation systems containing cytochromes, proteins and ascorbic acid were studied at physiological pH (7.4) under O2 or N2 with added H2O2. Proteins inhibited aromatic hydroxylation of p-nitrophenol or oxidative demethylation of ethylmorphine in ascorbic acid-containing systems incubated under O2, but strongly activated the systems containing H2O2. Cytochrome c and partially purified cytochrome P-450 from rat liver microsomal preparations activated the system in either O2 or H2O2. The systems needed ascorbic acid (or other enol structures) for activation. Cytochrome iron participated probably in the activation of O2, whereas cytochrome protein participated in a free radical activation of H2O2 (or of O2).

Aromatic hydroxylation in PBN spin trapping by hydroxyl radicals and cytochrome P-450

2000 ◽  
Vol 28 (3) ◽  
pp. 345-350 ◽  
Author(s):  
Lester A Reinke ◽  
Danny R Moore ◽  
Hong Sang ◽  
Edward G Janzen ◽  
Yashige Kotake
Keyword(s):  
Hydroxyl Radicals ◽  
Spin Trapping ◽  
Aromatic Hydroxylation ◽  
Cytochrome P 450
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