Abstract
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1.
Succinate dehydrogenase is inhibited by citrate and β-hydroxybutyrate in a complex manner, both in mitochondria and submitochondrial particles. Kinetics of inhibition in the particles points to a competitive component in the mechanism involved.
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2.
Pyruvate, α-ketoglutarate, malate, and glutamate stimulate oxidation of succinate by mitochondria.
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3.
Stimulation by α-ketoglutarate and glutamate is not influenced by the presence of rotenone.
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4.
Stimulation by pyruvate is higher in the absence of rotenone and increases significantly in the presence of K+ and valinomycin. Pyruvate supplies in mitochondria reducing equivalents for malate dehydrogenase operating in the reverse direction-reduction of oxaloacetate to malate.
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5.
Stimulation by malate is higher in the presence of rotenone.
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Hillar, M., Lott, V. & Lennox, B. Correlation of the effects of citric acid cycle metabolites on succinate oxidation by rat liver mitochondria and submitochondrial particles. J Bioenerg Biomembr 7, 1–15 (1975). https://doi.org/10.1007/BF01558459
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DOI: https://doi.org/10.1007/BF01558459