Summary
Comparison of the amino acid sequence worked out for the Ip subunit of succinate dehydrogenase from cardiac mitochondria with that of microbial enzyme and funarate dehydrogenase as well as ferredoxins suggests that all iron sulfur clusters in heart SDH may originally exist in the Ip.
It is now generally agreed that mitochondrial succinate dehydrogenase (SDH) (1) consists of two subunits which are separable by SDS-PAGE. The larger subunit contains covalently linked FAD with molecular weight of about 70,000 known as Fp and the smaller one approximately 27,000 called Ip contains only an iron-sulfur cluster without flavin. On the other hand, the distribution of iron-sulfur clusters is somewhat still not completely settled. Previously, it was thought that Fp contains FAD together with two 2Fe2S centers and that Ip contains one 4Fe4S center (4). Very recently, from physical methods, a claim has been made that Fp consists of a 2Fe2S center and a 4Fe4S cluster, whereas Ip consists of a 3FeXS cluster (2, 3).
This communication inquires how much information can be obtained about the positions of prosthetic groups bound to a protein from its amino acid sequence. Ip from cardiac mitochondria has been used to deduce sane knowledge in this aspect.
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King, T.E. et al. (1987). Iron Cluster Sites of Cardiac Ip-Subunit of Succinate Dehydrogenase. In: Papa, S., Chance, B., Ernster, L. (eds) Cytochrome Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1941-2_40
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DOI: https://doi.org/10.1007/978-1-4613-1941-2_40
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