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Quarter field resonance and integer-spin/half-spin interaction in the EPR of Thermus thermophilus ferrodoxin. Possible new fingerprints for three iron clusters
Hagen, Wilfred R.; Dunham, William Richard; Johnson, Michael K.; Fee, James A.
1985-04-29
Citation:Hagen, Wilfred R., Dunham, William R., Johnson, Michael K., Fee, James A. (1985/04/29)."Quarter field resonance and integer-spin/half-spin interaction in the EPR of Thermus thermophilus ferrodoxin. Possible new fingerprints for three iron clusters." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 828(3): 369-374. <http://hdl.handle.net/2027.42/25700>
Abstract: We describe two new characteristics of the EPR of the seven-iron containing ferrodoxin from Thermus thermophilus. First, the reduced state of the 3Fe center, which has traditionally been considered to be EPR-silent, has been found to exhibit [Delta]m = 4 transition, which is unique for Fe-S centers. This signal is similar to that of high-spin Fe2+-EDTA and supports the suggestion that the ground electronic state of the 3Fe cluster is S = 2. Second, we have recorded the EPR spectrum of the fully reduced protein at 9 and 15 GHz and found that changes occur in the signal which are consistent with a weak electronic spin-spin interaction between the [4Fe-4S]+ (S = 1/2) and the reduced 3Fe center. A theoretical explanation is given for the observation of interaction signals with constant effective g values.