scholarly journals Reconstruction of the succinic oxidase system from two preparations, one deficient in succinic dehydrogenase, the other deficient in cytochrome oxidase

1954 ◽  
Vol 58 (1) ◽  
pp. 142-146 ◽  
Author(s):  
A. Tissières
Keyword(s):  
Cytochrome Oxidase ◽  
Succinic Dehydrogenase ◽  
The Other ◽  
Oxidase System

Effect of inhibitors on the activity of soluble succinic dehydrogenase and on the reconstitution of the succinic dehydrogenase-cytochrome system from its components

1960 ◽  
Vol 152 (947) ◽  
pp. 163-187 ◽  
Keyword(s):  
Methylene Blue ◽  
Cytochrome Oxidase ◽  
Molecular Oxygen ◽  
Heart Muscle ◽  
Succinic Dehydrogenase ◽  
Reversible Reaction ◽  
Muscle Preparation ◽  
Oxidase System ◽  
Sites Of Action ◽  
Phenazine Methosulphate

The succinic dehydrogenase-cytochrome system, which catalyzes the oxidation of suecinate to fumarate by molecular oxygen, was successfully reconstituted from soluble succinic dehydrogenase, soluble cytochrome c and a particulate heart-muscle preparation which is deprived of these components but contains cytochromes a 3 , a , c 1 and b and has a strong cytochrome oxidase activity. Although succinic dehydrogenase isolated in a soluble form by Singer and by Wang with their co-workers was identified by them as a flavoprotein compound containing one modified flavin adenine dinucleotide and 2 or 4 iron atoms, neither the function of the iron nor the structure and function of the flavin group have so far been satisfactorily elucidated. Soluble succinic dehydrogenase, unlike its endogenous form, is very unstable and catalyzes the oxidation of succinate by phenazine methosulphate or ferricyanide but not by cytochrome c or methylene blue. However, when soluble enzyme is re-incorporated within the particles of the heart-muscle preparation deprived of this enzyme, it becomes an integral part of the respiratory chain and re-acquires all the properties of its endogenous form, that is insolubility, stability and reactivity towards the cytochrome system and methylene blue. The succinic dehydrogenase-cytochrome system thus reconstituted, on addition of cytochrome c , actively catalyzes the oxidation of succinate by molecular oxygen. It shows normal oxidation and reduction of its cytochrome components and is susceptible to all inhibitors in the same way as is the succinic oxidase system of an untreated heart-muscle preparation. The comparative study of a soluble succinic dehydrogenase and a particulate succinic oxidase system revealed: (i) that pyrophosphate, like malonate and oxalacetate, acts as a competitive inhibitor of the succinic dehydrogenase itself; (ii) that narcotics have two sites of action: like antimycin they break the link between cytochromes b and c 1 and, unlike antimycin, they also inhibit, but to a lesser degree, the activity of succinic dehydrogenase; and (iii) that cyanide can react with three components of this system in three different ways: a rapid and perfectly reversible reaction with cytochrome oxidase, a slow and still reversible reaction with oxidized soluble cytochrome c and a slow, irreversible reaction with the succinic dehydrogenase itself. It was previously shown (Tsou 1951) that the incubation of heart-muscle preparation with cyanide irreversibly inhibited the oxidation of succinate via the cytochrome system or methylene blue. Although cyanide treatment of soluble succinic dehydrogenase does not inhibit its catalytic activity in the oxidation of succinate by phenazine methosulphate, it prevents the dehydrogenase from anchoring itself within the particles of the heart-muscle preparation deprived of this enzyme, and so the reconstitution of the particulate succinic oxidase system does not take place. As the cyanide effect of Tsou is slow, irreversible, sensitive to temperature, complete and can be prevented by reducing substances, such as succinate acting as a hydrogen donor, or sodium dithionite, but not by malonate or pyrophosphate, we postulated: (i) that this effect is due to an irreversible reduction by cyanide of a disulphide group of succinic dehydrogenase to one thiol and one thiocyanate group, and (ii) th at this disulphide group originates by a reversible oxidation of a dithiol group which is present in addition to, and differs in several respects from the dithiol group of Hopkins.

Histochemical Observations on the Succinic Dehydrogenase and Cytochrome Oxidase Activity in Pigeon Breast-muscle

1961 ◽  
Vol s3-102 (57) ◽  
pp. 131-141
Author(s):  
J. C. GEORGE ◽  
C. L. TALESARA
Keyword(s):  
Distribution Pattern ◽  
Cytochrome Oxidase ◽  
Oxidative Metabolism ◽  
Succinic Dehydrogenase ◽  
The Other ◽  
Breast Muscle ◽  
Strictly Anaerobic ◽  
Dehydrogenase System ◽  
The Individual ◽  
Mitochondrial Staining

Histochemical and cytochemical observations were made on the exact localization and distribution pattern of succinic dehydrogenase system and cytochrome oxidase in the pigeon breast-muscle by employing slightly modified methods. Succinic dehydrogenase activity, which was not detected earlier either histochemically or biochemically in the broad white fibres, was demonstrated by using a modified incubation medium under strictly anaerobic conditions, with neotetrazolium as the hydrogen acceptor. The size, localization, and distribution pattern of the histochemically demonstrable diformazan and indophenol blue granules showed a more or less close resemblance to the mitochondrial staining in the individual red as well as white fibres. The occurrence of high oxidative metabolism in the narrow red fibres was revealed by the presence of a large number of succinoxidase-positive granules in these fibres. On the other hand, the presence of fewer, smaller granules indicated very low oxidative metabolism in the broad white fibres. The presence of the fewer, smaller succinoxidase-positive granules in the broad white fibres nevertheless shows that these fibres too possess mitochondria where at least a certain amount of oxidative activity does take place, and that they are to be considered as analogous to the white fibres of the other vertebrate skeletal muscles. It is also suggested that these granules are to be considered as mitochondria in the general sense and that the distinction between sarcosomes and mitochondria as proposed by previous authors needs reconsideration.

Oxidative Activity of Aortic Tissue of Man, the Rabbit and the Dog, With Special Reference to Succinic Dehydrogenase and Cytochrome Oxidase

1958 ◽  
Vol 195 (2) ◽  
pp. 476-480 ◽  
Author(s):  
Nelicia Maier ◽  
Henry Haimovici
Keyword(s):  
Special Reference ◽  
Cytochrome Oxidase ◽  
Abdominal Aorta ◽  
Abdominal Segment ◽  
Species Difference ◽  
Succinic Dehydrogenase ◽  
Hepatic Tissue ◽  
Human Aorta ◽  
Aortic Tissue ◽  
Enzymatic Systems

Succinic dehydrogenase and cytochrome oxidase activities were determined in homogenates of three aortic segments (ascending and arch, descending thoracic, abdominal) and liver of man, the rabbit and the dog. Both enzymes exhibited the lowest activity in human aorta. Succinic dehydrogenase exhibited the highest activity in the thoracic aorta of the dog and intermediate activity in the latter's abdominal segment and the rabbit's aorta. Cytochrome oxidase, in contrast, exhibited the highest activity in the rabbit's aorta. A slight gradient of decreasing activity from thoracic to abdominal aorta was noted for cytochrome oxidase in both the rabbit and dog and for succinic dehydrogenase in the rabbit, whereas a significant decrease in the latter enzyme was noted in the abdominal segment of the dog. No gradient of activity was apparent in man. Liver exhibited the lowest activity for both enzymes in man, highest in the dog and intermediate in the rabbit. The above findings suggest a biologic species difference between the aorta of man, the rabbit and the dog, which may be partly ascribed to a difference in the components of the above two enzymatic systems. The same species difference holds true for hepatic tissue.

Succinic and Malic Oxidase in Gastric Hydrochloric Acid Production

1956 ◽  
Vol 187 (3) ◽  
pp. 427-431 ◽  
Author(s):  
Joseph J. Vitale ◽  
Oscar M. Jankelson ◽  
Patricia Connors ◽  
D. Mark Hegsted ◽  
Norman Zamcheck
Keyword(s):  
Gastric Mucosa ◽  
Guinea Pig ◽  
Succinic Dehydrogenase ◽  
Titratable Acidity ◽  
Spectrophotometric Analysis ◽  
Parietal Cells ◽  
Human Gastric Mucosa ◽  
City Hospital ◽  
Malic Dehydrogenase ◽  
Oxidase System

Effect of histamine on the activity of succinic oxidase and malic dehydrogenase was studied in guinea pig and human gastric mucosa. Human tissue was obtained through the surgical services of the Boston City Hospital. Control value for the succinic oxidase system of the proximal half of the guinea pig stomach was approximately 480 ( Qo2 (N) (µl O2/mg nitrogen/hr.)). After histamine, this value rose to 550 in 30 minutes with a simultaneous rise in titratable acidity of the stomach contents. Animals fasted for 72 hours had a Qo2 (N) of approximately 500 and after histamine a Qo2 (N) of 700 was observed. Spectrophotometric analysis of succinic dehydrogenase and cytochrome oxidase activities, two of the major components of the succinic oxidase system, revealed that both components are increased following histamine administration. Malic dehydrogenase, however, was not affected by histamine treatment. Succinic dehydrogenase was demonstrated by histochemical localization and was concentrated below the superficial mucous layer where parietal cells were abundant. Succinic oxidase activity of human gastric mucosa was demonstrable only in those specimens containing abundant parietal cells. This study confirms the view that HCl production by parietal cells is associated with aerobic metabolism and is perhaps under enzymatic control. The study suggests that the succinic oxidase system may be involved in the production or secretion of HCl.

scholarly journals The ultrastructural cytochemistry of lactic dehydrogenase, succinic dehydrogenase, dihydro-nicotinamide adenine dinucleotide diaphorase and cytochrome oxidase activities in hair cell mitochondria of the guinea pig cochlea.

1975 ◽  
Vol 23 (3) ◽  
pp. 216-234 ◽  
Author(s):  
G J Spector
Keyword(s):  
Hair Cell ◽  
Cytochrome Oxidase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Nicotinamide Adenine ◽  
Fixation Method ◽  
Inner Mitochondrial Membrane ◽  
Tetrazolium Chloride ◽  
Outer Compartment

The use of cinnamyl nitroblue tetrazolium chloride (DS-NBT) in dehydrogenase experiments (lactic dehydrogenase, succinic dehydrogenase, nicotinamide adenine dinucleotide diaphorase) and 3,3'-diaminobenzidine tetrahydrochloride (DAB) in cytochrome oxidase experiments indicated that mitochondrial oxidoreduction reactions from nicotinamide adenine dinucleotide to cytochrome oxidase are located on the inner mitochondrial membrane in the outer compartment and the intracristate spaces. These reactions behave according to the chemiosmotic hypothesis. The cochlear hair cell mitochondria are cytochemically indistinguishable from free liver mitochondria. The heterogeneous mitochondrial staining pattern is related to the osmolarity of the incubation media, solubility of the enzymes and pH of the medium, but not to the fixation method.

scholarly journals THE LOCALIZATION OF SUCCINIC DEHYDROGENASE, CYTOCHROME OXIDASE AND ADENOSINE TRIPHOSPHATASE IN CILIATED RESPIRATORY EPITHELIUM

1965 ◽  
Vol 13 (8) ◽  
pp. 677-683 ◽  
Author(s):  
HERTHA R. CRESS ◽  
ALEXANDER SPOCK ◽  
DUNCAN C. HEATHERINGTON
Keyword(s):  
Cytochrome Oxidase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Respiratory Epithelium ◽  
Ciliary Activity ◽  
Basal Bodies ◽  
Tissue Cultures ◽  
Respiratory Epithelial Cells ◽  
Respiratory Epithelial

Succinic dehydrogenase and cytochrome oxidase activities were found to be scattered throughout the cytoplasm of ciliated and nonciliated respiratory epithelial cells while ATPase activity was restricted to cilia and areas under the cilia in the regions of the ciliary basal bodies. In order to elucidate the role of ATPase further, tissue cultures of rabbit tracheal epithelium with beating cilia were incubated in a medium perfused with cigarette smoke which resulted in cessation of ciliary motility. Epithelium with beating cilia was positive for ATPase while the epithelium with nonbeating cilia was negative or only weakly positive in a few small scattered areas. The presence of ATPase in beating cilia and its absence in nonbeating cilia agree with biochemical and physiological studies suggesting an association between ATP and ciliary activity.

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