Succinate dehydrogenase from the bay mussel, Mytilus edulis.
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Animals↗
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Results for “Electron Transport Complex II”
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Reconstitution of respiratory chain enzyme systems. VI. Indispensability of succinate in the isolation mixture for the preparation of the reconstitutively active succinate dehydrogenase.
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Electron Transport↗
Site of interaction of 2-p-nitrophenyl-3-p-iodophenyl-5-tetrazolium chloride in the succinate oxidase system.
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Chlorides↗
The inhibitory effects of quinones on the succinic oxidase system of the respiratory chain.
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Electron Transport↗
The incorporation of 14C into succinate dehydrogenase and the heart-muscle preparation from their reactions with K14CN.
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Biochemical Phenomena↗
Reconstitution of respiratory-chain systems. VIII. Reconstitution of a succinate-cytochrome c reductase system.
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Cytochromes↗
SUCCINATE DEHYDROGENASE IN THE ERGOT FUNGUS CLAVICEPS PURPUREA.
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Ascomycota↗
REACTIONS OF CYTOCHROMES A AND A3 IN THE SUCCINATE OXIDASE SYSTEM.
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Cytochromes↗
FRAGMENTATION OF THE ELECTRON TRANSPORT CHAIN OF ESCHERICHIA COLI. PREPARATION OF A SOLUBLE FORMATE DEHYDROGENASE-CYTOCHROME B1 COMPLEX.
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Bacterial Proteins↗
THE EFFECT OF OXYGEN ON THE COMPOSITION AND ORGANISATION OF THE ELECTRON TRANSPORT SYSTEM OF YEAST.
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Candida↗
INHIBITION OF SUCCINATE OXIDATION BY BARBITURATES IN TIGHTLY COUPLED MITOCHONDRIA.
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Adenosine Triphosphatases↗
OXIDATIVE PHOSPHORYLATION IN FRACTIONATED BACTERIAL SYSTEMS. VIII. ROLE OF PARTICULATE AND SOLUBLE FRACTIONS FROM ESCHERICHIA COLI.
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Dinitrophenols↗
Differential investigation of the capacity of succinate oxidation in human skeletal muscle.
Procedures are described for the estimation of the succinate:ubiquinone oxidoreductase and succinate:phenazine methosulfate oxidoreductase activities in post-nuclear supernatants of human skeletal muscle homogenates using 2,6-dichlorophenol indophenol as the terminal electron acceptor. The influence of ionic strength and of sucrose upon these assays and upon the succinate:cytochrome c oxidoreductase activity has been investigated. Sucrose markedly interferes with the activation of the succinate dehydrogenase complex. Succinate:cytochrome c oxidoreductase activity and succinate:phenazine methosulfate oxidoreductase activity are inhibited by increasing concentrations of ions and of sucrose. Our results lead us to propose the existence of a single acceptor site for phenazine methosulfate at the succinate dehydrogenase complex, not involved in the physiological electron flux across ubiquinone. Estimation of the enzymatic activities mentioned above allows differential investigation of the functional integrity of a large part of the respiratory chain in patients suspected of suffering from a neuromuscular disorder.
2,6-Dichloroindophenol↗
The succinic dehydrogenase levels of the pectoral muscles of a few representative types of birds and a bat in relation to the fibre diameter, muscle weight and body weight.
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Animals↗
Biochemical and physiological changes associated with the postnatal development of the biceps brachii.
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Body Weight↗
AMINO ACID-DEPENDENT PYROPHOSPHATE EXCHANGE DURING THE LIFE CYCLE OF THE BLOWFLY LUCILIA CUPRINA.
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Adenosine Triphosphate↗
LATERAL GENICULATE NUCLEUS: HISTOLOGICAL AND CYTOCHEMICAL CHANGES FOLLOWING AFFERENT DENERVATION AND VISUAL DEPRIVATION.
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Atrophy↗
Pyridoxal phosphate-induced dissociation of the succinate: ubiquinone reductase.
Treatment of the soluble ubiquinone-deficient succinate: ubiquinone reductase with pyridoxal phosphate results in the inhibition of the carboxin-sensitive ubiquinone-reductase activity of the enzyme. The inactivation is prevented by the soluble homolog of ubiquinone (Q2) but is insensitive to the dicarboxylates interacting with the substrate binding site of succinate dehydrogenase. The reactivity of the pyridoxal phosphate-inhibited enzyme with different electron acceptors suggests that the observed inhibition is due to the dissociation of succinate dehydrogenase from the enzyme complex. The soluble succinate dehydrogenase was recovered in the supernatant after treatment of the insoluble succinate: ubiquinone reductase with pyridoxal phosphate. The data obtained strongly suggest the participation of amino groups in the interaction between succinate dehydrogenase and the ubiquinone reactivity conferring peptide within the complex.
Animals↗