PMID:7669047
| Citation |
Eliasson, R, Reichard, P, Mulliez, E, Ollagnier, S, Fontecave, M, Liepinsh, E and Otting, G (1995) The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy. Biochem. Biophys. Res. Commun. 214:28-35 |
|---|---|
| Abstract |
During the reduction of ribonucleotides with [3H]formate by the class III anaerobic ribonucleotide reductase from Escherichia coli tritium appears in water and not in the product deoxyribonucleotide. In D2O, 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. |
| Links |
PubMed Online version:10.1006/bbrc.1995.2252 |
| Keywords |
Deoxycytidine/chemistry; Escherichia coli/enzymology; Hydrogen/chemistry; Hydroxyl Radical/chemistry; Magnetic Resonance Spectroscopy; Ribonucleotide Reductases/chemistry; Stereoisomerism |
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