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Cell Mol Life Sci. 1998 Jul;54(7):684-95.

Ribonucleotide reductases and radical reactions.

Author information

1
Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, CNRS, Université J. Fourier, Grenoble, France. fontecav@cbcrb.ceng.cea.fr

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.

PMID:
9711234
DOI:
10.1007/s000180050195
[Indexed for MEDLINE]

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