Interactions of Organic Hydroperoxides with Heme Proteins

ŽÍDEK, Lukáš, Miroslav MACHALA a Ladislav SKURSKÝ. Interactions of Organic Hydroperoxides with Heme Proteins. Drug Metabolism and Drug Interactions. Tel Aviv: Freund Publishing House, Ltd., 1991, roč. 9, 3-4, s. 209-234. ISSN 0792-5077.

Základní údaje

Originální název

Interactions of Organic Hydroperoxides with Heme Proteins

Autoři

ŽÍDEK, Lukáš, Miroslav MACHALA a Ladislav SKURSKÝ

Vydání

Drug Metabolism and Drug Interactions, Tel Aviv, Freund Publishing House, Ltd. 1991, 0792-5077

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Další údaje

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

HYDROPEROXIDE (4-METHYLBENZYL); DECOMPOSITION; HYDROPEROXIDE (CUMYL); MONOOXYGENASE (CYTOCHROME P-450 - DEPENDENT); 7-ETHOXYRESORUFIN DEETHYLATION; HEMOPROTEINS

Štítky

7-ETHOXYRESORUFIN DEETHYLATION, decomposition, HEMOPROTEINS, HYDROPEROXIDE (4-METHYLBENZYL), HYDROPEROXIDE (CUMYL)

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Anotace

V originále

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.