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Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase

  • Tsoo E. King
  • Tomoko Ohnishi
  • Daryl B. Winter
  • J. T. Wu
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

Since the discovery of succinate dehydrogenase, this enzyme has remained as one of the, if not the, most colorful enzymes essential for mitochondrial electron transport. Perhaps because it is tenaciously attached to the membrane and “uniquely” reacts with electron acceptors, reports on the serious attempts of its solubilization did not appear until 1955. It is true that Tsou in 1950 definitively established the non-identity of succinate dehydrogenase and cytochrome b in the respiratory chain (1); this establishment dispersed and clarified a major confusion which otherwise might have hindered progress further. Nonetheless, even today the structure-function relationship of succinate dehydrogenase is still largely unknown. This paper will briefly review our work on a specific facet of the dehydrogenase, i. e. the iron-sulfur centers by biochemical and EPR studies.

Keywords

Succinate Dehydrogenase Acetone Powder Active Succinate Dehydrogenase Nonheme Iron Phenazine Methosulfate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Tsoo E. King
    • 1
    • 2
  • Tomoko Ohnishi
    • 1
    • 2
  • Daryl B. Winter
    • 1
    • 2
  • J. T. Wu
    • 1
    • 2
  1. 1.Dept. of Chemistry and Laboratory of BioenergeticsState University of New YorkAlbanyUSA
  2. 2.Dept. of Biochemistry and BiophysicsUniversity of PennsylvaniaPhiladelphiaUSA

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