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.

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)

Anotace

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.