Iron-sulfur interconversions in the anaerobic ribonucleotide reductase from Escherichia coli

@article{Mulliez1999IronsulfurII,
  title={Iron-sulfur interconversions in the anaerobic ribonucleotide reductase from Escherichia coli},
  author={Etienne Mulliez and Sandrine Ollagnier-de Choudens and Christian Meier and Marco Cremonini and Claudio Luchinat and Alfred X. Trautwein and Marc Fontecave},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={1999},
  volume={4},
  pages={614-620}
}
 The anaerobic ribonucleotide reductase from Escherichia coli contains an iron-sulfur cluster which, in the reduced [4Fe-4S]+ form, serves to reduce S-adenosylmethionine and to generate a catalytically essential glycyl radical. The reaction of the reduced cluster with oxygen was studied by UV-visible, EPR, NMR, and Mössbauer spectroscopies. The [4Fe-4S… CONTINUE READING