Dalmonte 2009 J Biol Chem: Difference between revisions
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{{Publication | {{Publication | ||
|title=Dalmonte ME, Forte E, Genova ML, Giuffrรจ A, Sarti P, Lenaz G (2009) Control of respiration by cytochrome c oxidase in intact cells: role of the membrane potential. J Biol Chem 284: 32331- | |title=Dalmonte ME, Forte E, Genova ML, Giuffrรจ A, Sarti P, Lenaz G (2009) Control of respiration by cytochrome c oxidase in intact cells: role of the membrane potential. J Biol Chem 284:32331-5. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19776013 PMID: 19776013] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/19776013 PMID: 19776013 Open Access] | ||
|authors=Dalmonte ME, Forte E, Genova ML, Giuffre A, Sarti P, Lenaz G | |authors=Dalmonte ME, Forte E, Genova ML, Giuffre A, Sarti P, Lenaz G | ||
|year=2009 | |year=2009 | ||
|journal=J | |journal=J Biol Chem | ||
|abstract=Metabolic control analysis was applied to intact HepG2 cells. The effect on the control coefficient of cytochrome ''c''ย oxidase (C''c''OX) over cell respiration of both the electrical (ฮฯ) and chemical (ฮpH) component of the mitochondrial transmembrane proton electrochemical gradient (ฮฮผH+) was investigated. The overall O<sub>2</sub> consumption and specific C''c''OX activity of actively phosphorylating cells were titrated with cyanide under conditions in which ฮฯ and ฮpH were selectively modulated by addition of ionophores. In the absence of ionophores, C''c''OX displayed a high control coefficient (CIV = 0.73), thus representing an important site of regulation of mitochondrial oxidative phosphorylation. A high control coefficient value (CIV = 0.85) was also measured in the presence of nigericin, i.e. when ฮฯ is maximal, and in the presence of nigericin and valinomycin (CIV = 0.77), when ฮฮผH+ is abolished. In contrast, C''c''OX displayed a markedly lower control coefficient (CIV = 0.30) upon addition of valinomycin, when ฮฯ is converted into ฮpH. These results show that ฮฯ is responsible for the tight control of C''c''OX over respiration in actively phosphorylating cells. | |abstract=Metabolic control analysis was applied to intact HepG2 cells. The effect on the control coefficient of cytochrome ''c''ย oxidase (C''c''OX) over cell respiration of both the electrical (ฮฯ) and chemical (ฮpH) component of the mitochondrial transmembrane proton electrochemical gradient (ฮฮผH+) was investigated. The overall O<sub>2</sub> consumption and specific C''c''OX activity of actively phosphorylating cells were titrated with cyanide under conditions in which ฮฯ and ฮpH were selectively modulated by addition of ionophores. In the absence of ionophores, C''c''OX displayed a high control coefficient (CIV = 0.73), thus representing an important site of regulation of mitochondrial oxidative phosphorylation. A high control coefficient value (CIV = 0.85) was also measured in the presence of nigericin, i.e. when ฮฯ is maximal, and in the presence of nigericin and valinomycin (CIV = 0.77), when ฮฮผH+ is abolished. In contrast, C''c''OX displayed a markedly lower control coefficient (CIV = 0.30) upon addition of valinomycin, when ฮฯ is converted into ฮpH. These results show that ฮฯ is responsible for the tight control of C''c''OX over respiration in actively phosphorylating cells. | ||
|keywords=Nigericin, Valinomycin, Cytochrome C oxidase,ย Membrane potential | |keywords=Nigericin, Valinomycin, Cytochrome C oxidase,ย Membrane potential | ||
|mipnetlab=IT | |mipnetlab=IT Rome Sarti P, IT Bologna Lenaz G, IT Bologna Genova ML | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Human, Rat | |organism=Human, Rat | ||
|tissues=Liver | |tissues=Liver | ||
|preparations=Intact | |preparations=Intact cells | ||
|enzymes=Complex IV; | |enzymes=Complex IV;cytochrome c oxidase | ||
|instruments=Oxygraph-2k | |||
}} | }} |
Latest revision as of 11:20, 21 January 2020
Dalmonte ME, Forte E, Genova ML, Giuffrรจ A, Sarti P, Lenaz G (2009) Control of respiration by cytochrome c oxidase in intact cells: role of the membrane potential. J Biol Chem 284:32331-5. |
Dalmonte ME, Forte E, Genova ML, Giuffre A, Sarti P, Lenaz G (2009) J Biol Chem
Abstract: Metabolic control analysis was applied to intact HepG2 cells. The effect on the control coefficient of cytochrome c oxidase (CcOX) over cell respiration of both the electrical (ฮฯ) and chemical (ฮpH) component of the mitochondrial transmembrane proton electrochemical gradient (ฮฮผH+) was investigated. The overall O2 consumption and specific CcOX activity of actively phosphorylating cells were titrated with cyanide under conditions in which ฮฯ and ฮpH were selectively modulated by addition of ionophores. In the absence of ionophores, CcOX displayed a high control coefficient (CIV = 0.73), thus representing an important site of regulation of mitochondrial oxidative phosphorylation. A high control coefficient value (CIV = 0.85) was also measured in the presence of nigericin, i.e. when ฮฯ is maximal, and in the presence of nigericin and valinomycin (CIV = 0.77), when ฮฮผH+ is abolished. In contrast, CcOX displayed a markedly lower control coefficient (CIV = 0.30) upon addition of valinomycin, when ฮฯ is converted into ฮpH. These results show that ฮฯ is responsible for the tight control of CcOX over respiration in actively phosphorylating cells. โข Keywords: Nigericin, Valinomycin, Cytochrome C oxidase, Membrane potential
โข O2k-Network Lab: IT Rome Sarti P, IT Bologna Lenaz G, IT Bologna Genova ML
Labels:
Organism: Human, Rat
Tissue;cell: Liver
Preparation: Intact cells
Enzyme: Complex IV;cytochrome c oxidase
HRR: Oxygraph-2k