Ribonucleotide reductases and radical reactions |
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Authors: | M Fontecave |
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Institution: | (1) Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DBMS-CEA, CNRS, Université J. Fourier, 17 Avenue des Martyrs, F-38054 Grenoble Cedex 9 (France), Fax +33 4 76 88 91 24, e-mail: fontecav@cbcrb.ceng.cea.fr, FR |
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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.
Received 3 December 1997; received after revision 26 February 1998; accepted 27 February 1998 |
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Keywords: | , Ribonucleotide reductase, tyrosyl, glycyl, thiyl, radicals, hydroxyurea, nucleoside analogues, nitric oxide, superoxide,,,,,radical, |
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