Ribonucleotide reductases and radical reactions

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

Abstract

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

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@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} }