The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: structure, assembly, radical initiation, and evolution.

@article{Bollinger2008TheMC,
  title={The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: structure, assembly, radical initiation, and evolution.},
  author={J Martin Bollinger and Wei Jiang and Michael T. Green and Carsten Krebs},
  journal={Current opinion in structural biology},
  year={2008},
  volume={18 6},
  pages={650-7}
}
The catalytic mechanism of a class I ribonucleotide reductase (RNR) is initiated by the generation of a hydrogen-abstracting thiyl radical via a conformationally gated, proton-coupled electron-transfer (PCET) from a cysteine residue in the alpha(2) subunit over approximately 35A to the cofactor in the beta(2) subunit. A chain of aromatic amino acids that spans the two subunits mediates this long-distance PCET by the formation of transient side-chain radicals. Details of the conformational… CONTINUE READING