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Inactivation of firefly (P. pyralis) luciferase by phenylglyoxal. D. Gareth Rees*; Anthony T. Andrews University of Wales Institute, Cardiff, School of Applied Sciences, Colchester Avenue, Cardiff, CF23 9XR, U.K.      *(gdrees@uwic.ac.uk) Firefly luciferase is inactivated by phenylglyoxal (PGO), a reagent that tends to selectively modify chemically activated, functional arginines in proteins. Ligands partially protected the enzyme against inactivation in the order MgSO4 < [no addition, adenosine] < [D-luciferin, D-luciferin + MgSO4] << [AMP, AMP + MgSO4, ATP] << ATP + MgSO4. Overall, the simplest interpretation of this evidence is that the residue(s) attacked by PGO are near to the luciferin binding site but are primarily involved in the binding of the phosphate portions of adenosine nucleotides. Unambiguous assignment of a binding role is not possible at this stage however, since limited structural analysis suggested that the enzyme is in a non-native state following modification. The results from RP-HPLC/ES-MS analysis of tryptic peptides of native and PGO modified luciferase will be reported. [Poster: rees.dgaret.74482]

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