Aurintricarboxylic acid and polynucleotides as novel inhibitors of ribonucleotide reductases.
Ribonucleoside diphosphate reductases isolated from Escherichia coli, baker's yeast, Ehrlich ascites tumor cells, and unicellular green alga (Scenedesmus obliquus) are inhibited strongly and uniformly by the polymeric triphenylmethane dye, aurintricarboxylic acid. The molecule appears to interact simultaneously with the enzyme's various nucleotide and catalytic (iron-organic radical) sites. Oligo- and polyribonucleotides are also inhibitory. These reactions serve as models of the probably physiologic regulation of ribonucleotide reduction exerted by natural inhibitors. Partial characterization of an inhibitor fraction found in wheat seed embryo is described.
D000818:Animals; D001312:Aurintricarboxylic Acid / Q000494:pharmacology*; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology; D000460:Chlorophyta / Q000201:enzymology; D003509:Cyclohexanecarboxylic Acids / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D051379:Mice; D011119:Polynucleotides / Q000494:pharmacology*; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013329:Structure-Activity Relationship
D003509:Cyclohexanecarboxylic Acids; D011119:Polynucleotides; D001312:Aurintricarboxylic Acid; D012264:Ribonucleotide Reductases