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. 2010 Jun-Jul;1797(6-7):939-44.
doi: 10.1016/j.bbabio.2010.02.013. Epub 2010 Feb 17.

What are the sources of hydrogen peroxide production by heart mitochondria?

Vera G Grivennikova  1 , Alexandra V Kareyeva, Andrei D Vinogradov
Affiliations

What are the sources of hydrogen peroxide production by heart mitochondria?

Vera G Grivennikova et al. Biochim Biophys Acta. 2010 Jun-Jul.

Abstract

Coupled rat heart mitochondria produce externally hydrogen peroxide at the rates which correspond to about 0.8 and 0.3% of the total oxygen consumption at State 4 with succinate and glutamate plus malate as the respiratory substrates, respectively. Stimulation of the respiratory activities by ADP (State 4-State 3 transition) decreases the succinate- and glutamate plus malate-supported H2O2 production 8- and 1.3-times, respectively. NH4+ strongly stimulates hydrogen peroxide formation with either substrate without any effect on State 4 and/or State 3 respiration. Rotenone-treated, alamethicin-permeabilized mitochondria catalyze NADH-supported H2O2 production at a rate about 10-fold higher than that seen in intact mitochondria under optimal (State 4 succinate-supported respiration in the presence of ammonium chloride) conditions. NADH-supported hydrogen peroxide production by the rotenone-treated mitochondria devoid of a permeability barrier for H2O2 diffusion by alamethicin treatment are only partially (approximately 50%) sensitive to the Complex I NADH binding site-specific inhibitor, NADH-OH. The residual activity is strongly (approximately 6-fold) stimulated by ammonium chloride. NAD+ inhibits both Complex I-mediated and ammonium-stimulated H2O2 production. In the absence of stimulatory ammonium about half of the total NADH-supported hydrogen peroxide production is catalyzed by Complex I. In the presence of ammonium about 90% of the total hydrogen peroxide production is catalyzed by matrix located, ammonium-dependent enzyme(s).

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Figures

Fig. 1
Fig. 1
Limited permeability of mitochondrial membranes for hydrogen peroxide. Trace 1, Mitochondria (Mito) (1.8 mg/ml) were added to the standard reaction mixture in a closed vessel with oxygen-sensitive electrode and oxygen consumption and production were followed. The additions were: G+M, glutamate and malate 5 mM each; ADP 2 mM; Rot, rotenone 5 μM; H2O2 1 mM; Ala, alamethicin 40 μg/ml and MgCl2 2.5 mM. Trace 2, alamethicin and MgCl2 were added just before hydrogen peroxide. Trace 3, control, no mitochondria were added. The numbers (in italics) at the traces show the rates of oxygen consumption or production in two-electron equivalents per min per mg protein.
Fig. 2
Fig. 2
Distribution of the total NADH-supported hydrogen peroxide generating activities between the membrane-bound and matrix proteins in rat heart mitochondria. Mitochondria were treated, fractionated, and assayed as described in Table 3.
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