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https://open.uns.ac.rs/handle/123456789/14569
Nаziv: | Mechanism of reduction of nitrofurantoin on liver microsomes | Аutоri: | Leskovac V. Popović M. |
Dаtum izdаvаnjа: | 1-јан-1980 | Čаsоpis: | Pharmacological Research Communications | Sažetak: | Reduction of the nitro-group of nitrofurantoin /N-[5-Nitro-2-furfuryliden-] 1-aminohydantoin/ on liver microsomes is supported both by NADPH and NADH. The site of interaction of nitrofurantoin with microsomes appears to be on two flavoproteins, NADPH-cytochrome P450 reductase and NADH-cytochrome b5 reductase; interaction with the former enzyme is much stronger then with the later. Cytochromes P450 and b5 are not the sites of nitro-reduction. Aerobic and anaerobic fate of nitro-group is different. Under aerobic conditions, nitrofurantoin serves as a cyclic catalyst for the HAD/P/H-supported reduction of molecular oxygen to water; it becomes only catalytically reduced to nitro-anion free radical. Under anaerobic conditions, nitrofurantoin is permanently reduced by NAD/P/H; we were able to identify two successive reduction products of nitro-group, nitroso- and hydroxylamine-group. Normal redox potential of the nitro/nitroso redox couple is approx. O.O Volts. Under physiological conditions, nitrofurantoin, in addition to its transformations into stable reduction products, has a substantial draining effect on the HADPH-, NADH- and O2-pool in liver cells. A stronger cytotoxicity of nitrofurantoin should be expected under aerobic, compared to anaerobic conditions. © 1980 The Italian Pharmacological Society. | URI: | https://open.uns.ac.rs/handle/123456789/14569 | ISSN: | 00316989 | DOI: | 10.1016/S0031-6989(80)80058-0 |
Nаlаzi sе u kоlеkciјаmа: | TF Publikacije/Publications |
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