Objectives: Coenzyme Q(10), incorporated in DOPC lyposomes or naturally present in liver bovine mitochondria or in human blood plasma, was reacted with nitrogen dioxide (NO2)-N-center dot or with a (NO)-N-center dot/(NO2)-N-center dot mixture. Methods and Results: The reaction course was monitored by Electron Paramagnetic Resonance (EPR) spectroscopy and in all cases the formation of a di-tert-alkyl nitroxide was observed, deriving from the addition of (NO2)-N-center dot to one of the double bonds, most likely the terminal one, of the isoprenic chain. The rate constant for nitroxide formation was also determined by EPR spectroscopy and an initial rate of ca. 7 x 10(-8 )M s(-1) was obtained.
Reaction of endogenous Coenzyme Q10 with nitrogen monoxide and its metabolite nitrogen dioxide / Astolfi, P.; Clement, J. -L.; Gigmes, D.; Armeni, T.; Carloni, P.; Greci, L.. - In: REDOX REPORT. - ISSN 1351-0002. - ELETTRONICO. - 24:1(2019), pp. 56-61. [10.1080/13510002.2019.1647005]
Reaction of endogenous Coenzyme Q10 with nitrogen monoxide and its metabolite nitrogen dioxide
Astolfi P.
;Armeni T.;Carloni P.;Greci L.
2019-01-01
Abstract
Objectives: Coenzyme Q(10), incorporated in DOPC lyposomes or naturally present in liver bovine mitochondria or in human blood plasma, was reacted with nitrogen dioxide (NO2)-N-center dot or with a (NO)-N-center dot/(NO2)-N-center dot mixture. Methods and Results: The reaction course was monitored by Electron Paramagnetic Resonance (EPR) spectroscopy and in all cases the formation of a di-tert-alkyl nitroxide was observed, deriving from the addition of (NO2)-N-center dot to one of the double bonds, most likely the terminal one, of the isoprenic chain. The rate constant for nitroxide formation was also determined by EPR spectroscopy and an initial rate of ca. 7 x 10(-8 )M s(-1) was obtained.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
