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Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism

  • B. -M. Sjöberg
Chapter
Part of the Structure and Bonding book series (volume 88)

Abstract

Ribonucleotide reductases catalyze an essential reaction in all living cells — the production of deoxyribonucleotide precursors for DNA synthesis. An intricate allosteric regulation enables one and the same enzymic component to accept both purine and pyrimidine ribonucleotide substrates and to furnish growing cells with balanced deoxyribonucleotide pools. The reaction, which is based on radical chemistry, is common to all ribonucleotide reductases, whereas the mode of furnishing the radical differs and is currently a basis for distinguishing at least three different classes of ribonucleotide reductases. The radical generating components, although of seemingly different evolutionary origin, all include transition metal binding sites. Studies on the ribonucleotide reductase family highlight exciting mechanistic and evolutionary implications of far-reaching significance.

Keywords

ribonucleotide reductase diiron-oxo iron-sulfur tyrosyl radical glycyl radical ] S-adenosylmethionine 

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Copyright information

© Springer Verlag 1997

Authors and Affiliations

  • B. -M. Sjöberg
    • 1
  1. 1.Department of Molecular BiologyStockholm UniversityStockholmSweden

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