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- W2060703146 abstract "The mechanism of inhibition of the enzyme activity of mitochondrial malate dehydrogenase by thyroxine, iodine cyanide and molecular iodine has been further investigated. The results obtained allow us to exclude formation of a protein/inhibitor stable complex, iodination of the enzyme or disaggregation of the protein molecule into inactive subunits as explanations for the enzyme inactivation induced by the iodine-containing compounds. On the other hand, it has been demonstrated that in all cases the enzyme inhibition is dependent on the oxidation of certain—SH groups necessary for the activity. Direct oxidation of the thiol groups of the protein by molecular iodine and iodine cyanide can be easily assumed, whereas the chemical mechanism of the thyroxine-induced enzyme inactivation is harder to explain. However, since neither hormone deiodination nor metal chelation occur, while thyroxine by itself is also able to oxidize the thiol group of reduced glutathione, a direct effect of thyroxine on the sulfhydryl groups of the enzyme is postulated." @default.
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- W2060703146 date "1970-04-01" @default.
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- W2060703146 title "The Nature of Inhibition of Mitochondrial Malate Dehydrogenase by Thyroxine, Iodine Cyanide and Molecular Iodine" @default.
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- W2060703146 doi "https://doi.org/10.1111/j.1432-1033.1970.tb00932.x" @default.
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