Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site.

@article{Logan1996CrystalSO,
  title={Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site.},
  author={Derek T Logan and Xiao di Su and Anna {\AA}berg and Karin Regnstr{\"o}m and J{\'a}nos Hajdu and Hans Eklund and Paer Nordlund},
  journal={Structure},
  year={1996},
  volume={4 9},
  pages={1053-64}
}
BACKGROUND 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… CONTINUE READING

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