Abstract
A Co(II)-substituted form of the R2 protein of ribonucleotide reductase from Escherichia coli has been prepared by anaerobic addition of 4 equiv of Co(II) to the R2 apo protein in order to explore structural changes that may occur when divalent metal ions are coordinated in the metal binding sites. The visible absorption and circular dichroism spectra of the Co(II)-substituted R2 protein contain multiple absorption features in the 500-600-nm region with two apparent maxima at 515 and 550 nm (e 550 =115 M -1 cm -1 /Co(II)) indicative of Co(II) in a five-coordinate environment consisting of nitrogen or oxygen ligands
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