EurekaMag.com logo
+ Site Statistics
References:
52,725,316
Abstracts:
28,411,598
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

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


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



Related references

The circular dichroism and optical absorbancy of the histidyl flavine during active nonactive transition of soluble succinate dehydrogenase. Febs Letters 104(2): 371-375, 1979

The circular dichroism and optical absorbancy of the histidyl flavin during active-non-active transition of soluble succinate dehydrogenase. Febs Letters 104(2): 371-375, 1979

New properties of Bacillus subtilis succinate dehydrogenase altered at the active site. The apparent active site thiol of succinate oxidoreductases is dispensable for succinate oxidation. Biochemical Journal 260(2): 491-497, 1989

Studies on succinate dehydrogenase 8 alpha histidyl fad as the active center of succinate dehydrogenase. European Journal of Biochemistry 26(2): 279-289, 1972

Studies on succinate dehydrogenase. 8 -Histidyl-FAD as the active center of succinate dehydrogenase. European Journal of Biochemistry 26(2): 279-289, 1972

An antimycin-insensitive succinate-cytochrome c reductase activity in pure reconstitutively active succinate dehydrogenase. Biochimica et Biophysica Acta 893(1): 75-82, 1987

The transition between Makran subduction and the Zagros collision; recent advances in its structure and active deformation. Geological Society Special Publications 330: 43-64, 2010

Mechanism of the first steps of succinate oxidation by the mammalian succinate dehydrogenase. Schaefer, G (Ed ) Icsu (International Council Of Scientific Unions) Short Reports, Vol 3 Third European Bioenergetics Conference; Hannover, West Germany, Sept 2-7, 1984 Xlviii+745p Cambridge University Press: New York, N Y , Usa; Cambridge, England Illus 212-213, 1985

Reconstitution of respiratory chain enzyme systems. VI. Indispensability of succinate in the isolation mixture for the preparation of the reconstitutively active succinate dehydrogenase. Biochimica et Biophysica Acta 59: 492-494, 1962

Computational simulations of the interactions between acetyl-coenzyme-A carboxylase and clodinafop: resistance mechanism due to active and nonactive site mutations. Journal of Chemical Information and Modeling 49(8): 1936-1943, 2009