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Figure 7


Fig. 7. Schematic of the mitochondrial respiratory chain showing the effect of CO binding (x) at the terminal oxidase on hydrogen peroxide (H2O2) production. CO slows the rate of electron transport (solid arrows), enabling electrons to accumulate, including at complex III. Complex III and the proton motive Q cycle have been expanded to show sites of ubi-semiquinone (Q·-) formation from which electrons can be donated to produce superoxide (·O2-) (dotted arrows). Complex III O2 availability is also increased by CO, which promotes ·O2-production and its conversion to H2O2 by SOD2 (MnSOD). SOD2 induction may increase the extra-mitochondrial H2O2 leak rate. Cyt, cytochrome; ISP, iron sulfur protein; Q, oxidized coenzyme; QH2, reduced coenzyme Q. The details of the Q cycle, including the transmembrane proton flux, have been omitted for clarity.





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