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Interactions of Organic Hydroperoxides with Heme Proteins

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ŽÍDEK Lukáš MACHALA Miroslav SKURSKÝ Ladislav

Rok publikování 1991
Druh Článek v odborném periodiku
Časopis / Zdroj Drug Metabolism and Drug Interactions
Fakulta / Pracoviště MU

Přírodovědecká fakulta

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