Pyridoxal phosphate-induced dissociation of the succinate: ubiquinone reductase

Z. M. Choudhry, E. V. Gavrikova, Alexander Kotlyar, P. R. Tushurashvili, A. D. Vinogradov*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)171-175
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - 11 Mar 1985
Externally publishedYes


  • succinate dehydrogenase and the ubiquinone reactivity conferring peptide within the complex. Succinate: ubiquinone reductase Respiratory chain Enzyme modification


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