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  • succinate dehydrogenase  (3)
  • heart succinate dehydrogenase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Study of the interaction of cadmium with membrane-bound succinate dehydrogenase (1991)
    Springer
    Journal of bioenergetics and biomembranes 23 (1991), S. 381-389 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondria ; phosphorylating electron transport particles ; succinate dehydrogenase ; heart succinate dehydrogenase ; respiratory chain ; cadmium ; substrate-binding site
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Cadmium ions inhibit membrane-bound succinate dehydrogenase with a second-order rate constant of 10.42 mM−1s−1 at pH 7.35 and 25°C. Succinate and malonate protect the enzyme against cadmium ion inhibition. The protection pattern exerted by succinate and malonate suggests that the group modified by cadmium is located at the active site. The pH curve of inactivation by Cd2+ indicates the involvement of an amino acid residue with pKa of 7.23.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762229
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  • 2
    Electronic Resource
    Electronic Resource
    Inhibition of membrane-bound succinate dehydrogenase by fluorescamine (1993)
    Springer
    Journal of bioenergetics and biomembranes 25 (1993), S. 685-688 
    Details
    ISSN: 1573-6881
    Keywords: Fluorescamine ; succinate dehydrogenase ; heart mitochondria ; submitochondrial particles ; primary amine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Fluorescamine rapidly inactivated membrane-bound succinate dehydrogenase. The inhibition of the enzyme by this reagent was prevented by succinate and malonate, suggesting that the group modified by fluorescamine was located at the active site. The modification of the active site sulfhydryl group by 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB) did not alter the inhibitory action of fluorescamine. However, the protective effect of malonate against fluorescamine inhibition was abolished in the enzyme modified at the thiol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00770255
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibition of membrane-bound succinate dehydrogenase by disulfiram (1991)
    Springer
    Journal of bioenergetics and biomembranes 23 (1991), S. 335-343 
    Details
    ISSN: 1573-6881
    Keywords: Disulfiram ; antabuse ; heart mitochondria ; submitochondrial particles ; succinate dehydrogenase ; sulfhydryl groups
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of disulfiram on succinate oxidase and succinate dehydrogenase activities of beef heart submitochondrial particles was studied. Results show that disulfiram inhibits both functions. Succinate and malonate suppress the inhibitory action of disulfiram when succinate dehydrogenase is stabilized in an active conformation. Disulfiram is not able to inhibit the enzyme when succinate dehydrogenase is inactivated by oxaloacetate. The inhibitory effect of disulfiram is reverted by the addition of dithiothreitol. From these results, it is proposed that disulfiram inhibits the utilization of succinate by a direct modification of an -SH group located in the catalytically active site of succinate dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762226
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