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The incomplete inactivation of ribonuclease A (RNase A) by a fluoride (4) is a mechanism-based multiphasic kinetic process that facilitates the synthesis of other RNase A inhibitors. The rate of inactivation is not increased when the concentration of compound 4 is greater than 200 micromoles. Side chains of Lys7, Arg10, Gln69 and Glu111 are the preferred sites of inactivation. Inhibitor 4 is obtained by the reduction of a triester by sodium borohydride and subsequent fluorination with (diethylamino)sulfur trifluoride and TMSBr. The catalytic activity and synthesis of RNase A are discussed.

Dehydrohalogenation of associated 2-halo phosphates with metal amides provided 1-bromo enol phosphates and 1-benzoyloxy enol phosphates, novel phosphate esters with potential applications in the development of phosphatase and phosphodiesterase inactivators. These reactions involve a complex-include proximity effect. The dibromide resulted in 99% yield from the bromination of diethyl vinyl phosphate.