| Popis: |
Oxidation of semiquinone by O2 in the Q cycle is known to be one of the sources of Superoxide anion (O·2 -) in aerobic cells. In this paper, such a phenomenon was analyzed using the chemical kinetics model of electron transfer from succinate to Q·--cytochrome c, including coenzyme Q, the complex III non-heme iron protein FeS III and cytochromes b l, b h and c l Electron transfers from QH 2 to FeS III and cytochrome b l were assumed to occur according to direct transfer mechanism (dynamic channelling) involving the formation of FeS red III Q·-and Q·+-cytochrome b l complexes. For oxidation/reduction reactions involving cytochromes b h and b l, the dependence of the equilibrium and elementary rate constants on the membrane potential (Δψ) was taken into consideration. The rate of O·2 + generation was found to increase dramatically with increase in △ψ above the values found in State 3. On the other hand, the rate of cytochrome c reduction decreased sharply at the same values of the membrane potential. This explains experimental data that the O·2 + generation at State 4 appears to be very much faster than at State 3. A mild uncoupling in State 4 can markedly decrease the Superoxide generation due to a decrease in Δψ below the above mentioned critical level. ΔpH appears to be equally effective as Δψ in stimulation of superoxide production which depends, in fact, upon the Δμ(Mol Cell Biochem 184: 21–33, 1998) |
