Ribonucleotide reductase: no longer confusing but still amazing

W. Van Der Donk, S. Licht, D. Da Salva, J. McCarthy, M. J. Robins, J. Stubbe

Research output: Contribution to journalArticlepeer-review

Abstract

Ribonucleotide reductases catalyze the conversion of all nucleotides to deoxynucleotides, an essential step in DNA biosynthesis. Evidence will be presented, using rapid-freeze quench (RFQ) EPR -methods that a thiyl radical is generated in a kinetically competent fashion. Further evidence will be presented using RFQ EPR methods and 2' fluoromethylidene-nucleotides with RNRs that the function of the thiyl radical is to abstract a 3' hydrogen atom of the substrate. The first evidence for 3'-substrate derived radical will be presented. Thus, while the subtle details of the nucleotide reduction may never be known, the studies presented provide substantial support for the model proposed by Stubbe and co-workers in 1990 for a general mechanism of nucleotide reduction, subsequent to the generation of a transient protein radical.

Original languageEnglish (US)
Pages (from-to)A1086
JournalFASEB Journal
Volume10
Issue number6
StatePublished - Dec 1 1996
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Fingerprint

Dive into the research topics of 'Ribonucleotide reductase: no longer confusing but still amazing'. Together they form a unique fingerprint.

Cite this