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Recent advances on the mechanism of the active nonactive transition of succinate dehydrogenase


, : Recent advances on the mechanism of the active nonactive transition of succinate dehydrogenase. Journal of Molecular Catalysis 14(2): 185-196

The regulation of succinate dehydrogenase, which is achieved by a single negative modulator, oxaloacetate, and a variety of positive modulators (substrates, anions, reduced quinone and reduction) was studied at the molecular level. The fundamental difference between active and non-active enzyme appears to be a lowered redox potential of the flavin prosthetic group which prevents its reduction by substrate. Two mechanisms are proposed for the process by which oxaloacetate lowers the redox potential. Inorganic anions, which activate the deactivated enzyme, also appear to inhibit the enzyme already activated by succinate. This effect can be achieved by 2 different mechanisms, depending on the concentration of succinate, which involve respectively 1 or 2 Br ions.


Accession: 006269233

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Related references

Gutman M.; Bonomi F.; Pagani S.; Cerletti P., 1979: The circular dichroism and optical absorbancy of the histidyl flavine during active nonactive transition of soluble succinate dehydrogenase. Febs Letters 104(2): 371-375

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