The preparation of a novel phosphorus species, thiophosphoramidate, has ena
bled the specific thiophosphorylation of histidine at its 3-position. The r
ates of phosphorylation and thiophosphorylation of histidine are reported,
as well as the spectroscopic properties of both thiophosphoramidate and 3-t
hiophosphohistidine. Structural assignment of the latter was made by analog
y to the NMR properties of the known 3-phosphohistidine. The alkylation of
3-thiophosphohistidine by phenacyl bromide serves as a model for the introd
uction of labeling or probe reagents into histidine phosphorothioate-contai
ning proteins.