On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3'-C--H bond cleavage.
The 3'-carbon--hydrogen bond of [3'-3H]uridine 5'-diphosphate is cleaved during its conversion to 2'-deoxyuridine 5'-diphosphate catalyzed by Esherichia coli ribonucleoside diphosphate reductase. A selection against 3H of approximately 3.3 is observed on this reduction reaction. During the course of this reaction, a small but significant amount of 3H is released to the solvent.
D002250:Carbon Radioisotopes; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D011865:Radioisotope Dilution Technique; D012262:Ribonucleoside Diphosphate Reductase / Q000378:metabolism*; D012264:Ribonucleotide Reductases / Q000378:metabolism*; D014316:Tritium; D014530:Uridine Diphosphate
D002250:Carbon Radioisotopes; D014316:Tritium; D014530:Uridine Diphosphate; D012264:Ribonucleotide Reductases; D012262:Ribonucleoside Diphosphate Reductase