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Results for “SUCCINOXIDASE”

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At least 19 recordsLinked to original sources

PubMed1978

Reconstitution of escherichia coli succinoxidase from soluble components.

1. The membrane-bound succinoxidase of Escherichia coli was fractionated with deoxycholate into three soluble components, viz. succinate dehydrogenase.cytochrome b1 complex, cytochrome oxidase complex, and a factor identified as a phospholipid-containing component. 2. The dehydrogenase and cytochrome oxidase complexes were partially purified by filtration on Amicon membranes, Sepharose 4B chromatography, and sucrose gradient centrifugation. 3. Reconstitution of membranous succinoxidase, which catalyzes the oxidation of succinate by molecular oxygen by an integrated CN(-)-sensitive pathway, was achieved by mixing the soluble succinate dehydrogenase.cytochrome b1 complex with the soluble cytochrome oxidase complex in the presence of deoxycholate and then removing the detergent by gel filtration on Sephadex G-75. The phospholipid-containing factor stimulated the formation of succinoxidase by about 100% over that observed with the two complexes. 4. Isopycnic sucrose gradient centrifugation of succinate dehydrogenase.cytochrome b1 complex, cytochrome oxidase, and the reconstituted succinoxidase gave buoyant densities (p value) as 1.167, 1.229, and 1.194, respectively. 5. Electron microscopic evidence is presented for the vesicular nature of the reconstituted succinoxidase.

Cell Membrane↗

PubMed1992

Photoactivation of hypericin generates singlet oxygen in mitochondria and inhibits succinoxidase.

Photosensitized inhibition of mitochondrial succinoxidase by hypericin was measured in vitro and found to be drug-dose, light-dose, and wavelength dependent. Singlet oxygen generation, monitored using the singlet oxygen trap tetramethylethylene, and oxygen consumption in isolated mitochondria sensitized by hypericin were also light-dose and wavelength dependent. Unequivocal evidence for the generation of singlet oxygen was obtained using kinetic isotope ratios of products from the reaction between singlet oxygen and geminally deuterated tetramethylethylene. An action spectrum for the inhibition of succinoxidase was measured at wavelengths between 400 and 700 nm and found to parallel the recorded visible absorption spectrum of hypericin in isolated mitochondria. The greatest singlet oxygen generation, oxygen consumption, and succinoxidase inhibition occurred with white light or 600 nm irradiation. These data are consistent with a type II singlet-oxygen-mediated mechanism for hypericin induced photosensitized inhibition of mitochondrial succinoxidase.

Animals↗

PubMedDate not supplied

Inhibition of mitochondrial NADH oxidase, succinoxidase, and ATPase by naturally occurring flavonoids.

A structure-activity investigation of the inhibition of beef heart mitochondrial NADH oxidase and succinoxidase and rat liver mitochondrial ATPase by flavonoids was conducted. NADH oxidase was the most sensitive to inhibition by flavonoids: 13 of the 18 flavonoids tested inhibited NADH oxidase, whereas only 4 and 5 flavonoids inhibited succinoxidase and ATPase, respectively. The flavonoids possessing a catechol or pyrogallol moiety, and a 2,3-double bond and a 3-hydroxyl group were the most inhibitory towards the respiratory chain enzymes. The catechol or pyrogallol moiety did not exert preferential activity towards the oligomycin-sensitive ATPase because morin, which contains a meta-dihydroxy configuration, was the most potent ATPase inhibitor.

Adenosine Triphosphatases↗

PubMed1954

Cellular mechanisms of protein metabolism in the nephron. IV. The partition of succinoxidase and cytochrome oxidase activities in the cells of the proximal convolution of the rat after intraperitoneal injection of egg white.

1. Shifts of enzymatic activity have been followed during the formation and evolution of the droplets that form in the cells of the proximal convolution of the nephron of the rat after the injection of a 50 per cent solution of egg white in isotonic saline. 2. Twelve hours after injection there is a 35 to 40 per cent decrease in succinoxidase and cytochrome oxidase activities in the fraction containing the larger particles; i.e. mitochondria and droplets in equal concentration. Although after 30 hours the quantitative proportion of droplets and mitochondria is the same as previously, the activities of the fraction have returned to the normal observed originally in the uninjected rat in a corresponding fraction consisting of mitochondria only. 3. The microsome fraction shows an average increase of 35 per cent in oxidative enzyme activities during the early period following injection, and decreases to the original figure in the later period of droplet formation. 4. It is concluded from the shifting pattern of localization of oxidative enzyme activity within the cell particulates that the absorption droplets arise by the incorporation of the mitochondrial elements, which originally contain the highest enzyme activity, with absorbed protein through the intermediate stage of smaller (microsomal) particles.

Animals↗

PubMed1955

Relationship between the activity of the succinoxidase system and the rate of oxygen consumption during the embryonic development of the mealworm, Tenebrio molitor Linnaeus.

1. Readings were made on the rates of oxygen consumption and on the activities of the succinoxidase system of eggs of the mealworm for each day of embryonic development at 30 degrees C. 2. The rate of oxygen consumption, expressed as microliters/50 eggs/hour, was low (4.89) in newly laid eggs. It rose to 7.41 during the next 24 hours, remained at this level for the next 2 days, and then increased during the remainder of the embryonic period reaching a high value of 14.79 at the time of hatching. 3. The activity of cytochrome oxidase in eggs from newly emerged beetles, expressed as Delta log [Cy Fe(++)]/minute, remained at a value of 0.042 during the first half of the embryonic period, increasing to 0.233 during the latter half of this period. 4. The activity of succinic dehydrogenase showed the same series of changes except at much lower values. Expressed as Delta log [Cy Fe(+++)]/minute, they ranged from 0.010 in the newly laid egg to 0.034 at the end of the embryonic period. 5. The activity of cytochrome oxidase of the egg was found to decrease with parental age. Eggs from newly emerged beetles had activity values considerably higher than those of beetles 6 or 8 weeks after emergence. However, no comparable changes were noted in the activity of succinic dehydrogenase or in the rate of oxygen consumption. These observations suggest that cytochrome oxidase is not a rate-limiting enzyme in the respiratory metabolism of the mealworm egg.

Animals↗

PubMed1947