Harnessing free radicals: formation and function of the tyrosyl radical inribonucleotide reductase

Citation
J. Stubbe et P. Riggs-gelasco, Harnessing free radicals: formation and function of the tyrosyl radical inribonucleotide reductase, TRENDS BIOC, 23(11), 1998, pp. 438-443
Citations number
45
Categorie Soggetti
Biochemistry & Biophysics
Journal title
TRENDS IN BIOCHEMICAL SCIENCES
ISSN journal
09680004 → ACNP
Volume
23
Issue
11
Year of publication
1998
Pages
438 - 443
Database
ISI
SICI code
0968-0004(199811)23:11<438:HFRFAF>2.0.ZU;2-1
Abstract
Ribonucleotide reductases (RNRs) are uniquely responsible for converting nu cleotides to deoxynucleotides in all organisms. The cofactor of class-I RNR s comprises a di-iron cluster and a tyrosyl radical, and is essential for i nitiation of radical-dependent nucleotide reduction. Recently, much progres s has been made in understanding the mechanism by which this cofactor is ge nerated in vitro and in vivo, as well as the function of the tyrosyl radica l in nucleotide reduction. The Escherichia coli RNR cofactor provides a par adigm for cofactors in other di-iron requiring or tyrosyl-radical-requiring proteins.