PMID:9711234
| Citation |
Fontecave, M (1998) Ribonucleotide reductases and radical reactions. Cell. Mol. Life Sci. 54:684-95 |
|---|---|
| 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. |
| Links | |
| Keywords |
Binding Sites/physiology; DNA/biosynthesis; Enzyme Inhibitors/chemistry; Free Radicals/metabolism; Models, Molecular; Oxidation-Reduction; Ribonucleotide Reductases/chemistry; Ribonucleotide Reductases/classification; Ribonucleotides/metabolism |
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