The high potential iron-sulfur center in Escherichia coli fumarate reductase is a three-iron cluster.
The fumarate reductase complex and soluble enzyme from Escherichia coli have been investigated by low temperature magnetic circular dichroism and electron paramagnetic resonance spectroscopies. The results confirm the presence of one [2Fe-2S] cluster and show that the high potential iron-sulfur center is a 3Fe cluster of the type found in bacterial ferredoxins. Since the 3Fe cluster is present in catalytically competent enzyme and does not appear to be involved in any type of cluster conversion under reducing conditions, we conclude that it is an intrinsic component of the functional enzyme. The significance of the results is discussed in relation to the published amino acid sequence and the iron-sulfur cluster composition of bacterial fumarate reductases.
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003545:Cysteine / Q000032:analysis; D004227:Dithionite / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology*; D007506:Iron-Sulfur Proteins / Q000032:analysis*; D008667:Metalloproteins / Q000032:analysis*; D009097:Multienzyme Complexes / Q000032:analysis*; D013385:Succinate Dehydrogenase / Q000032:analysis*; D013696:Temperature
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D009097:Multienzyme Complexes; D004227:Dithionite; C033727:fumarate reductase complex; D013385:Succinate Dehydrogenase; D003545:Cysteine