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Succinate Dehydrogenase

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succinate dehydrogenase [¦sək·sə‚nāt ‚dē·hī′dräj·ə‚nās]
(biochemistry)
A key enzyme in the citric acid cycle; it oxidizes succinate to fumarate.

Succinate Dehydrogenase 

an enzyme of the oxidoreductase class that is prevalent in plant and animal cells, where it is localized in the inner membrane of mitochondria. Succinate dehydrogenase is one of the important enzymes involved in energy metabolism. In the tricarboxylic acid cycle, it catalyzes the reversible oxidation of succinic acid (succinate) to fumaric acid. The oxidation of one mole of succinic acid results in the synthesis of two moles of adenosine triphosphate (ATP). The electrons are transmitted from succinate dehydrogenase to the respiratory chain through coenzyme Q.

Succinate dehydrogenase, isolated in 1954 by the American scientist T. Singer, is structurally a flavoprotein; the protein constituent is covalently bound to the coenzyme flavin adenine dinucleotide (FAD). The enzyme contains eight atoms of nonheme iron as well as labile sulfur atoms. Sulfhydryl groups are believed to constitute part of the active center of succinate dehydrogenase.

REFERENCES

Lehninger, A. Biokhimiia. Moscow, 1974. (Translated from English.)
Singer, T. P., E. B. Kearney, and W. C. Kenney. “Succinate Dehydrogenase.” In Advances in Enzymology and Related Subjects of Biochemistry, vol. 37. New York, 1973.

V. V. ZUEVSKII



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The capacity of classic markers for mitochondrial density, ie, the capacity of citrate synthase (CS) and succinate dehydrogenase (SDH), as well the capacity of cytochrome c oxidase (COX) and beta-hydroxyacyl-CoA dehydrogenase (HAD), was determined in homogenized muscle biopsy samples obtained from the vastus lateralis muscle of nonexercising healthy young (age 20 [+ or -] 2 yr) subjects (31 women, 7 men).
Our working hypothesis is that tryptamine inhibits succinate dehydrogenase (SDH), a Krebs cycle enzyme that converts succinate to fumerate ultimately increasing ATP levels.
A Qualitative and Quantitative Assessment in Muscle Succinate dehydrogenase (SDH) has frequently been used as a qualitative histochemical marker for the presence of "ragged-red fibers" in skeletal muscle, which indicates abnormally increased numbers of mitochondria; this defect also is detected by the modified Gomori trichrome stain.
 
 
 
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