scholarly journals Thermodynamic control of electron flux through mitochondrial cytochrome bc1 complex

1985 ◽  
Vol 225 (2) ◽  
pp. 399-405 ◽  
Author(s):  
G C Brown ◽  
M D Brand

The redox states of exogenously added ubiquinone-2 and cytochrome c, and the protonmotive force (delta p) of rat liver mitochondria were measured as the respiration rate was titrated with the uncoupler carbonyl cyanide p-trifluoromethoxyphenyl-hydrazone. The force ratio delta Eh/delta p across the bc1 complex was close to 1:1 in State 4, indicating an H+/e- stoichiometry of 1:1 for the cytochrome bc1 complex, excluding protons moved by pool ubiquinone. Assuming a constant stoichiometry the rate of electron transport increased linearly with the disequilibrium (delta Eh - delta p) across the complex.

1985 ◽  
Vol 225 (2) ◽  
pp. 407-411 ◽  
Author(s):  
M D Brand ◽  
M K Al-Shawi ◽  
G C Brown ◽  
B D Price

Steady-state kinetic measurements showed that NN′-dicyclohexylcarbodi-imide decreased the observed H+/2e ratio of H+ transport by mitochondria respiring on succinate, acting mainly at the cytochrome bc1 complex. Thermodynamic assessment of the H+/2e ratio by measuring the force ratio across the bc1 complex showed that the inhibitor did not affect H+ translocation. Possible explanations of this disagreement between methods are examined; we conclude that the inhibitor does not alter the mechanistic stoichiometry of H+ pumping by the bc1 complex.


Sign in / Sign up

Export Citation Format

Share Document