Cookies help us deliver our services. By using our services, you agree to our use of cookies. More information

Quarato 2011 Biochim Biophys Acta

From Bioblast
Revision as of 11:14, 1 September 2011 by FriedenGagl Judith (talk | contribs) (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...")
(diff) โ† Older revision | Latest revision (diff) | Newer revision โ†’ (diff)
Publications in the MiPMap
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.

ยป PMID:21565165

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 (ฮ”ฮจ(m)) and the proton (ฮ”pH(m)) gradient, displayed a similar effect. Quantitative estimation of the ฮ”ฮจ(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. โ€ข Keywords: metabolic control analysis, oxidative phosphorylation, mitochondrial membrane potential, cytochrome c oxidase respiratory chain supercomplexes

โ€ข O2k-Network Lab: IT_Foggia_Capitanio N


Labels:


Organism: Human  Tissue;cell: Fibroblast  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