Fluorescence Studies of the Interaction of Nucleotides with the Active Site of the Nuclease of Staphylococcus aureus

In the late 1960s, Anfinsen's lab sought to understand the complicated details of the physicochemical properties of Staphylococcus aureus in solution, ultimately to better understand the relationship of its structure to its function. In this article, Anfinsen, Cuatrecasas, and Edelhoch reported that the specific binding of a competitive inhibitor resulted in a marked decrease in tyrosyl fluorescence, which they interpreted as indicative of a specific interaction of the nucleotide with several tyrosyl groups in the active site of the enzyme.