ESEEM studies of the iron-sulphur clusters of succinate dehydrogenase in Arum maculatum spadix mitochondrial membranes.

We have performed ESEEM spectroscopy in order to obtain structural information about the environment of the [2Fe-2S] cluster and the [3Fe-4S] cluster of succinate dehydrogenase (Centres 1 and 3, respectively) in intact Arum maculatum mitochondrial membranes. Both iron-sulphur clusters showed modulations indicative of 14N in the three-pulse echo decay envelopes. We have estimated the hyperfine couplings for the reduced [2Fe-2S] cluster (A approximately 1.1 MHz) and the oxidised [3Fe-4S] cluster (A approximately 0.8 MHz). Our results are compared with ESEEM data obtained for purified [2Fe-2S] cluster-containing proteins, namely Spirulina platensis ferredoxin, a protein for which the three-dimensional structure is known, and Escherichia coli fumarate reductase. The hyperfine and quadrupolar coupling parameters determined are consistent with a weak interaction of Centre 1 and Centre 3 with peptide 14N, rather than 14N of imidazole rings.