Fluoride, pyrophosphate, and base release from 2'-deoxy-2'-fluoronucleoside 5'-diphosphates by ribonucleoside-diphosphate reductase.

Ribonucleoside-diphsophate reductase from Escherichia coli catalyzes release of fluoride, inorganic pyrophosphate, and base from 2'-deoxy-2'-fluoronucleoside diphosphates. This reaction is accompanied by inactivation of the enzyme and an increase in absorbance at 314 nm of the inactivated protein. 2'-Deoxy-2'-fluoroadenosine 5'-diphosphate requires two turnovers per inactivation, whereas 2'-deoxy-2'-fluorocytidine 5'-diphosphate requires 100 turnovers per inactivation.