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Eliasson, R.; Reichard, P.; Mulliez, E.; Ollagnier, S.; Fontecave, M.; Liepinsh, E.; Otting, G.
Biochemical and biophysical research communications, 09/1995, Letnik: 214, Številka: 1Journal Article
During the reduction of ribonucleotides with 3Hformate by the class III anaerobic ribonucleotide reductase from Escherichia coli tritium appears in water and not in the product deoxyribonucleotide. In D 2O, deuterium replaces the OH-group at carbon-2′ with retention of configuration. In addition we find 1-2 % deuterium in the 3′-position demonstrating a small exchange of this hydrogen with the protons of water during catalysis. Class I and II enzymes catalyze identical reactions. Members of the three classes of reductases apparently use the same chemical mechanism in spite of having completely different protein structures.
