Skip to main content
. 2013 May 23;1(1):304–312. doi: 10.1016/j.redox.2013.04.005

Table 1.

Reduction levels of reporters and corresponding calculated rates of H2O2 production from site IF and site IIIQo in the presence of different substrates and inhibitors. With each substrate, the redox states of NAD(P)H and cytochrome b566 were measured in parallel with the measurements of overall rates of H2O2 production reported in Fig. 5. Eqs. (2) and (3) describing the calibration curves in Fig. 2 were used to calculate the rates of superoxide/H2O2 production from site IF and site IIIQo from these redox measurements. Concentrations of substrates and inhibitors are given in Fig. 5. All rates are in pmol H2O2 min−1 mg protein−1. Data are means±SEM (n≥4). Error values on the calculated rates of H2O2 production represent the propagated error as described in Materials and methods and Ref. [21].

Substrates and inhibitors Redox state of site IFreporter and calculated rate of superoxide/H2O2production by site IF
Redox state of site IIIQoreporter and calculated rate of superoxide/H2O2production by site IIIQo
Reduced NAD(P)H (%) Reported rate of H2O2 production Reduced cytochrome b566 (%) Reported rate of H2O2 production
Succinate 89±1 59±4 46±2 91±18
Succinate+rotenone 80±2 49±4 50±1 124±15
Glycerol 3-phosphate 59±3 34±6 29±2 27±7
Glycerol 3-phosphate+malonate 59±3 34±6 29±2 27±7
Glycerol 3-phosphate+malonate+rotenone 39±2 31±5 31±3 33±9
Palmitoylcarnitine+carnitine 80±1 49±4 42±3 72±18
Palmitoylcarnitine+carnitine+malonate 79±1 48±4 44±2 80±17
Glutamate+malate 85±7 54±9 38±5 54±18