Ribonucleotide reductases: radical chemistry and inhibition at the active site.
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.
Robins
Morris J
MJ
Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602-5700, USA. morris-robins@byu.edu
D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods; D007700:Kinetics; D012263:Ribonucleosides / Q000737:chemistry / Q000378:metabolism; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*
D012263:Ribonucleosides; D012264:Ribonucleotide Reductases