title: The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy.
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.
authors.affiliation: Department of Biochemistry 1, Medical Nobel Institute, MBB Karolinska Institute, Stockholm, Sweden.
authors.forename: R
authors.initials: R
authors.lastname: Eliasson
authors.forename: P
authors.initials: P
authors.lastname: Reichard
authors.forename: E
authors.initials: E
authors.lastname: Mulliez
authors.forename: S
authors.initials: S
authors.lastname: Ollagnier
authors.forename: M
authors.initials: M
authors.lastname: Fontecave
authors.forename: E
authors.initials: E
authors.lastname: Liepinsh
authors.forename: G
authors.initials: G
authors.lastname: Otting
mesh_terms: D003841:Deoxycytidine / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology*; D006859:Hydrogen / Q000737:chemistry; D017665:Hydroxyl Radical / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D012264:Ribonucleotide Reductases / Q000737:chemistry*; D013237:Stereoisomerism
chemical_list: D003841:Deoxycytidine; D017665:Hydroxyl Radical; D006859:Hydrogen; D012264:Ribonucleotide Reductases