Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.

@article{Eriksson1997BindingOA,
  title={Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.},
  author={M{\"a}rit Eriksson and Ulla Uhlin and Subramanyan Ramaswamy and Monica Ekberg and Karin Regnstr{\"o}m and Britt-Marie Sj{\"o}berg and Hans Eklund},
  journal={Structure},
  year={1997},
  volume={5 8},
  pages={1077-92}
}
BACKGROUND Ribonucleotide reductase (RNR) is an essential enzyme in DNA synthesis, catalyzing all de novo synthesis of deoxyribonucleotides. The enzyme comprises two dimers, termed R1 and R2, and contains the redox active cysteine residues, Cys462 and Cys225. The reduction of ribonucleotides to deoxyribonucleotides involves the transfer of free radicals. The pathway for the radical has previously been suggested from crystallographic results, and is supported by site-directed mutagenesis studies… CONTINUE READING
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