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Mutagenesis studies of stringently conserved firefly luciferase active site residues Bruce R. Branchini*; RA Magyar; MH Murtiashaw; NC Portier; M Zimmer Department of Chemistry, Connecticut College, 270 Mohegan Avenue, New London, CT 06320, USA      *(brbra@conncoll.edu) We have previously presented a potential model of the firefly luciferase active site complexed with its natural substrates luciferin and Mg-ATP. Using this model obtained by molecular modeling studies, we targeted several amino acids stringently conserved among 20 luciferase sequences for site-directed mutagenesis studies. We expressed, purified, and characterized the firefly luciferase enzymes containing changed amino acids at positions equivalent to Arg218, His245, Thr343, and Lys529 in the P. pyralis sequence. We will present the results of studies on: enzyme activity, bioluminescence color, steady state kinetic constants, and catalysis of the individual adenylation and oxidation partial reactions. The results will be discussed in the context of our model. [Talk: branchin.brucer.52131]

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