Ribonucleotide reductases: radical chemistry and inhibition at the active site
1Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602-5700, USA. morris-robins@byu.edu
Abstract:
Ribonucleoside 5'-diphosphate reductases (RDPRs) have been studied for several decades. Increasingly sophisticated mechanisms have been proposed for the reduction of natural substrate ribonucleotides to their 2'-deoxy counterparts and for mechanism-based inactivation of RDPRs with 2'-substituted-ribonucleotides. We now discuss biomimetic reactions of model substrate and inhibitor analogues, which clarify three aspects of previously proposed mechanisms postulated to occur at the active site of RDPRs.
Related Concept Videos
Radical Reactivity: Overview
Phase I Reactions: Reductive Reactions
Radical Reactivity: Nucleophilic Radicals
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Radical Reactivity: Intramolecular vs Intermolecular
Radical Reactivity: Steric Effects
Along with electronic factors, steric factors also account...


