Electron paramagnetic resonance spectroscopy (EPR) coupled to the spin trapping technique was used to detect carbon-centered radicals in rat liver mitochondria and submitochondrial particles exposed to t-butyl-hydroperoxide (TBH), using the spin trapping agent 3,5-dibromo-4-nitroso-benzenesulfonic acid (DBNBS). The signal recorded was unambiguously assigned to the methyl radical adduct. DBNBS was added to isolated rat liver mitochondria energized with succinate, and the methyl radical adduct was observed. The addition of NADH, NADPH, inhibitors of the respiratory chain, and of monoaminoxidase (MAO) inhibitors did not cause any relevant modification in the yield of radical adduct formation. Boiling and the addition of a non-ionic detergent inhibited the formation of the radical adduct, while experiments carried out under hypoxic conditions generated a significant increase in methyl radical formation. Further experiments were carried out on sub-mitochondrial particles (SMP) giving rise to, basically, the same results. From the above results, we are proposing that haem prosthetic groups are the likely source of TBH bioactivation in mitochondria.

t-Butyl-hydroperoxide bioactivation to methyl radical in rat liver mitochondria and submitochondrial particles / Iannone, Anna; Bini, A; JIN Y., G; Tomasi, Aldo; Vannini, V.. - In: FREE RADICAL RESEARCH COMMUNICATIONS. - ISSN 8755-0199. - STAMPA. - 19:(1993), pp. S141-S147.

t-Butyl-hydroperoxide bioactivation to methyl radical in rat liver mitochondria and submitochondrial particles

IANNONE, Anna;TOMASI, Aldo;
1993

Abstract

Electron paramagnetic resonance spectroscopy (EPR) coupled to the spin trapping technique was used to detect carbon-centered radicals in rat liver mitochondria and submitochondrial particles exposed to t-butyl-hydroperoxide (TBH), using the spin trapping agent 3,5-dibromo-4-nitroso-benzenesulfonic acid (DBNBS). The signal recorded was unambiguously assigned to the methyl radical adduct. DBNBS was added to isolated rat liver mitochondria energized with succinate, and the methyl radical adduct was observed. The addition of NADH, NADPH, inhibitors of the respiratory chain, and of monoaminoxidase (MAO) inhibitors did not cause any relevant modification in the yield of radical adduct formation. Boiling and the addition of a non-ionic detergent inhibited the formation of the radical adduct, while experiments carried out under hypoxic conditions generated a significant increase in methyl radical formation. Further experiments were carried out on sub-mitochondrial particles (SMP) giving rise to, basically, the same results. From the above results, we are proposing that haem prosthetic groups are the likely source of TBH bioactivation in mitochondria.
1993
19
S141
S147
t-Butyl-hydroperoxide bioactivation to methyl radical in rat liver mitochondria and submitochondrial particles / Iannone, Anna; Bini, A; JIN Y., G; Tomasi, Aldo; Vannini, V.. - In: FREE RADICAL RESEARCH COMMUNICATIONS. - ISSN 8755-0199. - STAMPA. - 19:(1993), pp. S141-S147.
Iannone, Anna; Bini, A; JIN Y., G; Tomasi, Aldo; Vannini, V.
File in questo prodotto:
Non ci sono file associati a questo prodotto.
Pubblicazioni consigliate

Licenza Creative Commons
I metadati presenti in IRIS UNIMORE sono rilasciati con licenza Creative Commons CC0 1.0 Universal, mentre i file delle pubblicazioni sono rilasciati con licenza Attribuzione 4.0 Internazionale (CC BY 4.0), salvo diversa indicazione.
In caso di violazione di copyright, contattare Supporto Iris

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/608597
Citazioni
  • ???jsp.display-item.citation.pmc??? 1
  • Scopus 8
  • ???jsp.display-item.citation.isi??? 6
social impact