PMID:8805591
| Citation |
Logan, DT, Su, XD, Aberg, A, Regnström, K, Hajdu, J, Eklund, H and Nordlund, P (1996) Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site. Structure 4:1053-64 |
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| Abstract |
Ribonucleotide reductases (RNRs) catalyze the formation of the deoxyribonucleotides that are essential for DNA synthesis. The R2 subunit of Escherichia coli RNR is a homodimer containing one dinuclear iron centre per monomer. A tyrosyl radical is essential for catalysis, and is formed via a reaction in which the reduced, diferrous form of the iron centre activates dioxygen. To help understand the mechanism of oxygen activation, we examined the structure of the diferrous form of R2. |
| Links | |
| Keywords |
Carboxylic Acids/chemistry; Crystallography, X-Ray; Iron/metabolism; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen/metabolism; Ribonucleotide Reductases/chemistry; Ribonucleotide Reductases/genetics; Ribonucleotide Reductases/metabolism |
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