Ribonucleotide reductases and radical reactions

  • Marc Fontecave
  • Published 1998 in Cellular and Molecular Life Sciences CMLS


Ribonucleotide reductases (RNRs) catalyse the reduction of ribonucleotides to deoxyribonucleotides. They play a pivotal role in the regulation of DNA synthesis and are targets for antiproliferative drugs. Ribonucleotide reductases are unique enzymes in that they all require a protein radical for activity. Class I nonheme iron RNRs (mammals, plants, Escherichia coli) use a tyrosyl/cysteinyl radical pair, class II adenosylcobalamin RNRs (prokaryotes, archaea) a cysteinyl radical, class III iron-sulphur RNRs (facultative anaerobes) a glycyl radical. Here we describe the reactivity of these radicals with respect to the natural ribonucleotide substrates as well as to a variety of enzyme inhibitors, radical scavengers, nitric oxide, superoxide radicals and substrate analogues.

DOI: 10.1007/s000180050195

6 Figures and Tables


Citations per Year

195 Citations

Semantic Scholar estimates that this publication has 195 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Fontecave1998RibonucleotideRA, title={Ribonucleotide reductases and radical reactions}, author={Marc Fontecave}, journal={Cellular and Molecular Life Sciences CMLS}, year={1998}, volume={54}, pages={684-695} }