Turacin and the supposed catalytic activity of copper-porphyrins

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Abstract
Turacin (Cu-uroporphyrin III) did not catalyse the oxidation of either ascorbic acid or cysteine. This great stability and unreactivity of turacin and the fact that its Cu did not combine with protein, made it difficult to visualize how a Cu-porphyrin could act as a prosthetic group of an oxidizing catalyst. The catalytic activity of Cu-porphyrins obtained by other workers was probably due to traces of free Cu left over from the prepn. of these compounds. Spectrophotometric studies were made of acid and alkaline turacin in the visible and near-violet regions of the spectrum. On increasing the degree of dispersion of the pigment, as for example with caffeine, the Soret band was shifted towards the longer wavelengths, i.e., in the opposite direction to the well known shift of the bands in the visible region of the spectrum. These findings were found to apply to several other porphyrin compounds examined. Turacin was not affected by bacteria (Bacillus subtilis), molds (Penicillium notatum and Aspergillus niger) or by passage through the kidney in the rat after parenteral admn.
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