Quarato 2011 Biochim Biophys Acta: Difference between revisions
(Created page with "{{Publication |title=Quarato G, Piccoli C, Scrima R, Capitanio N. (2011) Variation of flux control coefficient of cytochrome c oxidase and of the other respiratory chain complexe...") ย |
No edit summary |
||
| Line 7: | Line 7: | ||
|abstract=The metabolic control analysis was applied to digitonin-permeabilized HepG2 cell line to assess the flux control exerted by cytochrome c oxidase on the mitochondrial respiration. Experimental conditions eliciting different energy/respiratory states in mitochondria were settled. The results obtained show that the mitochondrial electrochemical potential accompanies a depressing effect on the control coefficient exhibited by the cytochrome c oxidase. Both the components of the protonmotive force, i.e. the voltage (ฮฮจ(m)) and the proton (ฮpH(m)) gradient, displayed a similar effect. Quantitative estimation of the ฮฮจ(m) unveiled that the voltage-dependent effect on the control coefficient of cytochrome c oxidase takes place sharply in a narrow range of membrane potential from 170-180 to 200-210mV consistent with the physiologic transition from state 3 to state 4 of respiration. Extension of the metabolic flux control analysis to the NADH dehydrogenase and bc(1) complexes of the mitochondrial respiratory chain resulted in a similar effect. A mechanistic model is put forward whereby the respiratory chain complexes are proposed to exist in a voltage-mediated threshold-controlled dynamic equilibrium between supercomplexed and isolated states. | |abstract=The metabolic control analysis was applied to digitonin-permeabilized HepG2 cell line to assess the flux control exerted by cytochrome c oxidase on the mitochondrial respiration. Experimental conditions eliciting different energy/respiratory states in mitochondria were settled. The results obtained show that the mitochondrial electrochemical potential accompanies a depressing effect on the control coefficient exhibited by the cytochrome c oxidase. Both the components of the protonmotive force, i.e. the voltage (ฮฮจ(m)) and the proton (ฮpH(m)) gradient, displayed a similar effect. Quantitative estimation of the ฮฮจ(m) unveiled that the voltage-dependent effect on the control coefficient of cytochrome c oxidase takes place sharply in a narrow range of membrane potential from 170-180 to 200-210mV consistent with the physiologic transition from state 3 to state 4 of respiration. Extension of the metabolic flux control analysis to the NADH dehydrogenase and bc(1) complexes of the mitochondrial respiratory chain resulted in a similar effect. A mechanistic model is put forward whereby the respiratory chain complexes are proposed to exist in a voltage-mediated threshold-controlled dynamic equilibrium between supercomplexed and isolated states. | ||
|keywords=metabolic control analysis, oxidative phosphorylation, mitochondrial membrane potential, cytochrome c oxidase respiratory chain supercomplexes | |keywords=metabolic control analysis, oxidative phosphorylation, mitochondrial membrane potential, cytochrome c oxidase respiratory chain supercomplexes | ||
|mipnetlab=IT_Foggia_Capitanio N ย | |mipnetlab=IT_Foggia_Capitanio N | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|organism=Human | |organism=Human, Mouse | ||
|tissues=Fibroblast | |tissues=Fibroblast, Hepatocyte; Liver | ||
|preparations=Intact Cell; Cultured; Primary | |preparations=Intact Cell; Cultured; Primary | ||
}} | }} | ||
Revision as of 14:10, 5 September 2011
| Quarato G, Piccoli C, Scrima R, Capitanio N. (2011) Variation of flux control coefficient of cytochrome c oxidase and of the other respiratory chain complexes at different values of protonmotive force occurs by a threshold mechanism. Biochim. Biophys. Acta.1807(9):1114-1124. |
Quarato G, Piccoli C, Scrima R, Capitanio N (2011) Biochim. Biophys. Acta
Abstract: The metabolic control analysis was applied to digitonin-permeabilized HepG2 cell line to assess the flux control exerted by cytochrome c oxidase on the mitochondrial respiration. Experimental conditions eliciting different energy/respiratory states in mitochondria were settled. The results obtained show that the mitochondrial electrochemical potential accompanies a depressing effect on the control coefficient exhibited by the cytochrome c oxidase. Both the components of the protonmotive force, i.e. the voltage (ฮฮจ(m)) and the proton (ฮpH(m)) gradient, displayed a similar effect. Quantitative estimation of the ฮฮจ(m) unveiled that the voltage-dependent effect on the control coefficient of cytochrome c oxidase takes place sharply in a narrow range of membrane potential from 170-180 to 200-210mV consistent with the physiologic transition from state 3 to state 4 of respiration. Extension of the metabolic flux control analysis to the NADH dehydrogenase and bc(1) complexes of the mitochondrial respiratory chain resulted in a similar effect. A mechanistic model is put forward whereby the respiratory chain complexes are proposed to exist in a voltage-mediated threshold-controlled dynamic equilibrium between supercomplexed and isolated states. โข Keywords: metabolic control analysis, oxidative phosphorylation, mitochondrial membrane potential, cytochrome c oxidase respiratory chain supercomplexes
โข O2k-Network Lab: IT_Foggia_Capitanio N
Labels:
Organism: Human, Mouse
Tissue;cell: Fibroblast, Hepatocyte; Liver"Hepatocyte; Liver" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.
Preparation: Intact Cell; Cultured; Primary"Intact Cell; Cultured; Primary" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
HRR: Oxygraph-2k
