On porphyrin esterification and ester hydrolysis. Studies on esterification of natural animal porphyrins with various alcohols and the acid hydrolysis of their esters.
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Saccharomyces cerevisiae mutants bearing mutations at the cyc4 locus are partially deficient in cytochrome synthesis. Although the mutation is not in the structural gene for delta-aminolevulinic acid (Alv) synthase, the mutants are deficient in Alv synthesis in vivo as indicated by abnormally low intracellular Alv concentrations. The cyc4 mutation causes cells to grow very slowly in minimal glucose medium, but not in yeast extract-peptone-glucose medium. A simple nutritional defect caused by the cyc4 mutation is not involved because cytochrome deficiency is enhanced by growing cyc4 cells in yeast extract-peptone medium. A regulatory role for CYC4 is indicated. Evidence for negative feed-back control of Alv synthase by heme is provided by the observation of enhanced intracellular Alv accumulation in yeast mutants partially deficient in decarboxylation of uroporphyrinogen and coproporphyrinogen, respectively.
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The authors report the experiments about incubation of uroporphyrinogen with sonified fibroblasts of normal individuals and prophyrics and present the hypothesis of the absence of deficiency in the activity of uroporphyrinogendecarboxylase.
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Targeted synthesis of the title compound, with one converging coordination site and three diverging H-bonding sites, has led to the formation of multiporphyrin oligomers by directed intermolecular coordination, without resorting to external auxiliaries. A uniquely structured cyclic tetraporphyrin supermolecule was detected in solution, isolated in the solid state, and characterized in detail by X-ray diffraction.