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Hydrogen peroxide generation by higher plant mitochondria oxidizing complex I or complex II substrates

Braidot E
•
Petrussa E
•
Vianello A
•
Macri F
1999
  • journal article

Periodico
FEBS LETTERS
Abstract
The generation of H2O2 by isolated pea stem mitochondria, oxidizing either malate plus glutamate or succinate, was examined. The level of H2O2 was almost one order of magnitude higher when mitochondria were energized by succinate. The succinate-dependent H2O2formation was abolished by malonate, but unaffected by rotenone. The lack of effect of the latter suggests that pea mitochondria were working with a proton motive force below the threshold value required for reverse electron transfer. The activation by pyruvate of the alternative oxidase was reflected in an inhibition of H2O2 formation. This effect was stronger when pea mitochondria oxidized malate plus glutamate. Succinate-dependent H2O2 formation was ca. four times lower in Arumsp. mitochondria (known to have a high alternative oxidase) than in pea mitochondria. An uncoupler (FCCP) completely prevented succinate-dependent H2O2 generation, while it only partially (40^50%) inhibited that linked to malate plus glutamate. ADP plus inorganic phosphate (transition from state 4 to state 3) also inhibited the succinate-dependent H2O2 formation. Conversely, that dependent on malate plus glutamate oxidation was unaffected by low and stimulated by high concentrations of ADP. These results show that the main bulk of H2O2is formed during substrate oxidation at the level of complex II and that this generation may be prevented by either dissipation of the electrochemical proton gradient (uncoupling and transition state 4-state 3), or preventing its formation (alternative oxidase). Conversely, H2O2 production, dependent on oxidation of complex I substrate, is mainly lowered by the activation of the alternative oxidase.
DOI
10.1016/S0014-5793(99)00616-X
WOS
WOS:000080704000027
SCOPUS
2-s2.0-0033046063
Archivio
http://hdl.handle.net/11390/719837
Diritti
closed access
Scopus© citazioni
70
Data di acquisizione
Jun 2, 2022
Vedi dettagli
Web of Science© citazioni
65
Data di acquisizione
Jun 3, 2022
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