Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P-450.
TLDR
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.About:
This article is published in Archives of Biochemistry and Biophysics.The article was published on 1976-08-01 and is currently open access. It has received 329 citations till now. The article focuses on the topics: Cumene hydroperoxide & Hydroxylation.read more
Citations
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Structure and Chemistry of Cytochrome P450
TL;DR: This review will concentrate on findings with P-450cam of the Pseudomonas putida camphor-5-exo-hydroxylase, and attention will be drawn to parallel and contrasting examples from other P- 450s as appropriate.
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Role of metals in oxygen radical reactions
TL;DR: Factors such as pH and chelation govern the reactivity of the transition metals with dioxygen and "oxy-radicals" and therefore influence the apparent mechanisms by which oxidative damage to phospholipids, DNA, and other biomolecules is initiated.
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Cytochromes P450 as versatile biocatalysts.
TL;DR: The set of interesting reactions being catalysed by cytochromes P450 systems and the availability of new genetic engineering techniques allowing to heterologously express them and to improve and change their activity, stability and selectivity makes them promising candidates for biotechnological application in the future.
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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.
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Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation.
TL;DR: The directed evolution of the P450 from Pseudomonas putida is reported to create mutants that hydroxylate naphthalene in the absence of cofactors through the ‘peroxide shunt’ pathway, with more than 20-fold higher activity than the native enzyme.
References
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Journal ArticleDOI
The Carbon Monoxide-binding Pigment of Liver Microsomes I. EVIDENCE FOR ITS HEMOPROTEIN NATURE
Tsuneo Omura,Ryo Sato +1 more
TL;DR: The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.
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The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
TL;DR: A chronology of key events leading up to and including the birth of Bonnichsen, R. K. & Bonner, J. (1952).
Journal Article
Spectral studies of drug interaction with hepatic microsomal cytochrome.
TL;DR: Two types of spectral changes are described as resulting from substrate interaction with a hepatic microsomal cytochrome; the magnitude of these spectral changes is dependent on protein concentration and substrate concentration as well as the substrate employed.
Journal Article
Biochemical and pharmacological changes in the rat following chronic administration of morphine, nalorphine and normorphine
Joseph Cochin,Julius Axelrod +1 more
TL;DR: The N-demethylating enzyme is proposed as a model for the study of narcotic-drug receptor sites and the degree of tolerance, cross-tolerance and depression of enzymatic activity depends on the amount of drug given per day rather than on the duration of drug administration.
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Role of Hemoprotein P-450 in Fatty Acid ω-Hydroxylation in a Soluble Enzyme System from Liver Microsomes
Anthony Y. H. Lu,Minor J. Coon +1 more
TL;DR: An enzyme system which catalyzes the ω-hydroxylation of fatty acids in the presence of reduced triphosphopyridine nucleotide and molecular oxygen has been obtained in a soluble form from rabbit liver microsomes.
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The Carbon Monoxide-binding Pigment of Liver Microsomes I. EVIDENCE FOR ITS HEMOPROTEIN NATURE
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