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J. Biol. Chem., Vol. 255, Issue 12, 5511-5513, Jun, 1980
JA Stubbe and JW Kozarich
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.
Fluoride, pyrophosphate, and base release from 2'-deoxy-2'- fluoronucleoside 5'-diphosphates by ribonucleoside-diphosphate reductase
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