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On the Role of Iron in the Linkage of Succinate Dehydrogenase to the Membrane

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Membrane-Bound Enzymes

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 14))

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Abstract

Little is known about the nature of the linkage between succinate dehydrogenase (succinate:(acceptor) oxidoreductase, EC 1.3. 99.1) and the inner mitochondrial membrane. A role of iron has been proposed on the basis of the solubilizing effect of cyanide and of hydroxyl ions on the flavoprotein (1). This action has been interpreted as due to replacement of a ligand in a non-heme coordination complex (1). Direct evidence for this interaction has so far been lacking but some relevant results on the point were recently obtained in our laboratory.

This work has been supported in part by grants from the Italian National Research Council.

Abbreviations: TTA, 2-thenoyltrifluoroacetone,4,4,4-trifluoro-1(2-thienyl) 1-3-butane-dione; DCPI, 2,6-dichlorophenolindophenol.

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Cerletti, P., Zanetti, G. (1971). On the Role of Iron in the Linkage of Succinate Dehydrogenase to the Membrane. In: Porcellati, G., di Jeso, F. (eds) Membrane-Bound Enzymes. Advances in Experimental Medicine and Biology, vol 14. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-4616-3_10

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  • DOI: https://doi.org/10.1007/978-1-4614-4616-3_10

  • Publisher Name: Springer, Boston, MA

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