Abstract
A rubredoxin-like mononuclear iron-sulfur derivative of adrenodoxin was prepared from the apoprotein and FeCl 3 in the presence of dithiothreitol. The mononuclear compound displayed optical absorption maxima at 276, 350, and 500 nm, and exhibited electron paramagnetic resonance absorption at g = 4.27 with a shoulder at g = 4.28, which can be ascribed to high spin ferric ion. From p-chloromercuriphenyl sulfonate titration experiments the iron atom appears to contain approximately one g atom of iron per mole of protein. This rubredoxin-like derivative was very unstable at 22° (the half-life was approximately 10 minutes), whereas the native 2 Fe2S∗ protein is known to be quite stable. This instability is believed to be intrinsic to the polypeptide sequence of adrenodoxin.
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