Difference between revisions of "Ragan 1975 J Biol Chem"
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{{Publication | {{Publication | ||
|title=Ragan CI, Hinkle PC (1975) Ion transport and respiratory control in vesicles formed from reduced nicotinamide adenine dinucleotide coenzyme Q reductase and phospholipids. J Biol Chem 250: 8472-8476. | |title=Ragan CI, Hinkle PC (1975) Ion transport and respiratory control in vesicles formed from reduced nicotinamide adenine dinucleotide coenzyme Q reductase and phospholipids. J Biol Chem 250: 8472-8476. | ||
|info=[http://www.jbc.org/content/250/21/8472.full.pdf+html PMID: 386 Open Access] | |info=[http://www.jbc.org/content/250/21/8472.full.pdf+html PMID: 386 Open Access] | ||
|authors=Ragan CI, Hinkle PC | |authors=Ragan CI, Hinkle PC | ||
| Line 6: | Line 6: | ||
|journal=J Biol Chem | |journal=J Biol Chem | ||
|abstract=NADH-coenzyme Q reductase from bovine heart mitochondria (complex I) was incorporated into phospholipid vesicles by the cholate dialysis procedure. Mixtures of purified phosphatidylcholine and phosphatidylethanolamine were required. Oxidation of NADH by coenzyme Q1 catalyzed by the reconstituted vesicles was coupled to proton translocation, directed inward, with an H+/2e ratio greater than 1.4. Similar experiments measuring proton translocation in submitochondrial particles gave an H+/2e ratio of 1.8. The proton translocation in both systems was not seen in the presence of uncoupling agents and was in addition to the net proton uptake from the reduction of coenzyme Q1 by NADH. Electron transfer in the reconstituted vesicles also caused the uptake of the permeant anion tetraphenylboron. The rate of electron transfer by the reconstituted vesicles was stimulated about 3-fold by uncouplers or by valinomycin plus nigericin and K+ ions. The results indicate that energy coupling can be observed with isolated NADH-coenzyme Q reductase if the enzyme complex is properly incorporated into a phospholipid vesicle. | |abstract=NADH-coenzyme Q reductase from bovine heart mitochondria (complex I) was incorporated into phospholipid vesicles by the cholate dialysis procedure. Mixtures of purified phosphatidylcholine and phosphatidylethanolamine were required. Oxidation of NADH by coenzyme Q1 catalyzed by the reconstituted vesicles was coupled to proton translocation, directed inward, with an H+/2e ratio greater than 1.4. Similar experiments measuring proton translocation in submitochondrial particles gave an H+/2e ratio of 1.8. The proton translocation in both systems was not seen in the presence of uncoupling agents and was in addition to the net proton uptake from the reduction of coenzyme Q1 by NADH. Electron transfer in the reconstituted vesicles also caused the uptake of the permeant anion tetraphenylboron. The rate of electron transfer by the reconstituted vesicles was stimulated about 3-fold by uncouplers or by valinomycin plus nigericin and K+ ions. The results indicate that energy coupling can be observed with isolated NADH-coenzyme Q reductase if the enzyme complex is properly incorporated into a phospholipid vesicle. | ||
|keywords=Ion transport, Respiratory control, NADH-coenzyme Q reductase, Phospholipids, Vesicles, Beef heart | |keywords=Ion transport, Respiratory control, NADH-coenzyme Q reductase, Phospholipids, Vesicles, Beef heart | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Mammals | |organism=Mammals | ||
|tissues= | |tissues=Heart | ||
|preparations=Isolated Mitochondria | |preparations=Isolated Mitochondria | ||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Revision as of 12:08, 27 February 2013
| Ragan CI, Hinkle PC (1975) Ion transport and respiratory control in vesicles formed from reduced nicotinamide adenine dinucleotide coenzyme Q reductase and phospholipids. J Biol Chem 250: 8472-8476. |
Ragan CI, Hinkle PC (1975) J Biol Chem
Abstract: NADH-coenzyme Q reductase from bovine heart mitochondria (complex I) was incorporated into phospholipid vesicles by the cholate dialysis procedure. Mixtures of purified phosphatidylcholine and phosphatidylethanolamine were required. Oxidation of NADH by coenzyme Q1 catalyzed by the reconstituted vesicles was coupled to proton translocation, directed inward, with an H+/2e ratio greater than 1.4. Similar experiments measuring proton translocation in submitochondrial particles gave an H+/2e ratio of 1.8. The proton translocation in both systems was not seen in the presence of uncoupling agents and was in addition to the net proton uptake from the reduction of coenzyme Q1 by NADH. Electron transfer in the reconstituted vesicles also caused the uptake of the permeant anion tetraphenylboron. The rate of electron transfer by the reconstituted vesicles was stimulated about 3-fold by uncouplers or by valinomycin plus nigericin and K+ ions. The results indicate that energy coupling can be observed with isolated NADH-coenzyme Q reductase if the enzyme complex is properly incorporated into a phospholipid vesicle. • Keywords: Ion transport, Respiratory control, NADH-coenzyme Q reductase, Phospholipids, Vesicles, Beef heart
Labels:
Organism: Mammals"Mammals" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Tissue;cell: Heart
Preparation: Isolated Mitochondria"Isolated Mitochondria" 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.
Made history
