Publication details
Interactions of Organic Hydroperoxides with Heme Proteins
| Authors | |
|---|---|
| Year of publication | 1991 |
| Type | Article in Periodical |
| Magazine / Source | Drug Metabolism and Drug Interactions |
| MU Faculty or unit | |
| Citation | |
| Keywords | HYDROPEROXIDE (4-METHYLBENZYL); DECOMPOSITION; HYDROPEROXIDE (CUMYL); MONOOXYGENASE (CYTOCHROME P-450 - DEPENDENT); 7-ETHOXYRESORUFIN DEETHYLATION; HEMOPROTEINS |
| Description | 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. |