Journal ArticleDOI
Kinetic study on enzymatic s-oxygenation promoted by a reconstituted system with purified cytochrome P-450
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Thioanisole derivatives were found to be oxygenated by a reconstituted system of purified cytochrome P-450 to give sulfoxides suggesting the oxygenation to proceed via one electron transfer from sulfides to the active species of the enzyme.About:
This article is published in Tetrahedron Letters.The article was published on 1980-01-01. It has received 104 citations till now. The article focuses on the topics: Thioanisole & Cytochrome.read more
Citations
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Journal ArticleDOI
Oxidizing species in the mechanism of cytochrome P450
TL;DR: In this paper, a review discusses the mechanisms of oxygen activation by cytochrome P450 enzymes, the possible catalytic roles of the various iron-oxygen species formed in the catalytic cycle, and progress in understanding the mechanism of hydrocarbon hydroxylation, heteroatom oxidation, and olefin epoxidation.
Journal ArticleDOI
Enzymatic oxidation of xenobiotic chemicals.
TL;DR: There is actually some commonality among many of the catalytic mechanisms of oxidation, even among proteins with different structures and prosthetic groups, and it is seen that cytochrome P-450 has some elements of a peroxidase and vice versa.
Book ChapterDOI
Substrate Oxidation by Cytochrome P450 Enzymes
TL;DR: The role of the ferric peroxo complex as an electrophilic oxidizing agent remains a matter of debate, as the evidence advanced in support of the proposal is circumstantial and contradictory.
Journal ArticleDOI
Role of Radical Cations in Aromatic Hydrocarbon Carcinogenesis
TL;DR: Evidence is provided for the involvement of one-electron oxidation in PAH carcinogenesis through binding of benzo[a]pyrene to mouse skin DNA, which occurs predominantly at C-6, the position of highest charge localization in the BP radical cation, and binding of 6-methyl BP to DNA in mouse skin yields a major adduct.
References
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Journal ArticleDOI
Hydroxylation and epoxidation catalyzed by iron-porphine complexes. Oxygen transfer from iodosylbenzene
Journal ArticleDOI
Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate
TL;DR: A very large isotope effect and a significant amount of epimerization for the hydroxylation of norbornane by cytochrome P-450, suggest an initial hydrogen abstraction to give a carbon radical intermediate.
Journal ArticleDOI
Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P-450.
TL;DR: Data obtained are in accord with a peroxidase-like mechanism for the action of cytochrome P-450, which catalyzes the hydroperoxide-dependent hydroxylation of a variety of substrates in the absence of NADPH, NADPHcytochromeP-450 reductase, and molecular oxygen.
Journal ArticleDOI
A gel-electrophoretically homogeneous preparation of cytochrome P-450 from liver microsomes of phenobarbital-pretreated rabbits
Yoshio Imai,Ryo Sato +1 more
TL;DR: Cytochrome P-450 was purified from liver microsomes of phenobarbital-pretreated rabbits to a specific content of 16 to 17 nmoles per mg of protein with a yield of about 10 %.
Journal ArticleDOI
Interaction of Peroxidases with Aromatic Peracids and Alkyl Peroxides PRODUCT ANALYSIS
Gregory R. Schonbaum,Siu Lo +1 more
TL;DR: The results establish that horseradish peroxidase (H-peroxidases) Compound I is not an enzyme peroxide complex, but a derivative in which the active site is oxidized.