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

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Book cover Iron and Copper Proteins

Part of the book series: Advances in Experimental Medicine and Biology ((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.

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King, T.E., Ohnishi, T., Winter, D.B., Wu, J.T. (1976). Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase. In: Yasunodu, K.T., Mower, H.F., Hayaishi, O. (eds) Iron and Copper Proteins. Advances in Experimental Medicine and Biology, vol 74. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3270-1_15

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