Abstract
Summary A weak EPR resonance at g = 2.015 has been observed in five oxidized Clostridial-type ferredoxins. Oxidized Clostridium acidi-urici [ 57 Fe] ferredoxin exhibited a broadened resonance at g = 2.015 relative to the signal from native or reconstituted [ 56 Fe]ferredoxin. This experiment, in conjunction with other results, demonstrates that the signal exhibited by oxidized Clostridial ferredoxin either originates from the Fe 4 S 4 * clusters of the protein or from a paramagnetic species bound to the clusters. Oxidized C. acidi-urici ferredoxin, when treated with the oxidant potassium ferricyanide, was found to exhibit an approximate 100 fold increase in the intensity of the signal. Results of experiments performed on the ferricyanide treated ferredoxin are consistent with the existence of a third oxidation state of the protein.
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