ŽÍDEK, Lukáš, Miroslav MACHALA and Ladislav SKURSKÝ. Interactions of Organic Hydroperoxides with Heme Proteins. Online. Drug Metabolism and Drug Interactions. Tel Aviv: Freund Publishing House, Ltd., 1991, vol. 9, 3-4, p. 209-234. ISSN 0792-5077. [citováno 2024-04-23]
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Basic information
Original name Interactions of Organic Hydroperoxides with Heme Proteins
Authors ŽÍDEK, Lukáš, Miroslav MACHALA and Ladislav SKURSKÝ
Edition Drug Metabolism and Drug Interactions, Tel Aviv, Freund Publishing House, Ltd. 1991, 0792-5077.
Other information
Type of outcome Article in a journal
Confidentiality degree is not subject to a state or trade secret
Organization unit Faculty of Science
Keywords in English HYDROPEROXIDE (4-METHYLBENZYL); DECOMPOSITION; HYDROPEROXIDE (CUMYL); MONOOXYGENASE (CYTOCHROME P-450 - DEPENDENT); 7-ETHOXYRESORUFIN DEETHYLATION; HEMOPROTEINS
Tags 7-ETHOXYRESORUFIN DEETHYLATION, decomposition, HEMOPROTEINS, HYDROPEROXIDE (4-METHYLBENZYL), HYDROPEROXIDE (CUMYL)
Changed by Changed by: prof. Mgr. Lukáš Žídek, Ph.D., učo 38990. Changed: 21/5/2001 10:46.
Abstract
The decomposition of p-methylbenzyl hydroperoxide by cytochrome c and other selected heme systems in the absence of reucing agents was investigated. p-Methylbenzaldehyde was identified as the major product. A mechanism for this reaction has been suggested. H2O2 and tertiary cumyl hydroperoxide do not react under these conditions. The ability of organic hydroperoxides to act as oxygen donors in the cytochrome-mediated 7-ethoxyresorufin-O-deethylation was studied. Cumyl and tert.butyl hydroperoxides are able to substitute oxygen in the absence of NADPH while p-methylbenzyl hydroperoxide is not.
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