The Fourier transforms of the laser-induced absorption decay from glycogen phosphorylase and DOPA decarboxylase.
Fourier analysis of the laser-induced absorption decay curves of 3,4-dihydroxyphenylalanine (DOPA) decarboxylase and glycogen phosphorylase demonstrates a powerful technique in the analysis of complicated decay behavior. Phosphorylase which uses the pyridoxal 5'-phosphate cofactor in an unknown manner exhibits over weak absorption an intense decay while decarboxylase demonstrates only weak absorption. Fourier analysis of the decay curves clearly shows that phosphorylase has an intense absorption decay in the midst of three weaker ones and that decarboxylase only has three weak decays. This conclusion justifies the isolation and use of the intense decay of phosphorylase as an observable in the study of protein dynamics at the active site about the cofactor. The decay has demonstrated a movement of positive charge to substrate in the mechanism of phosphorylation of glycogen units.
Ledbetter
J W
JW
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston 29425.
Lindroth
J R
JR
Martin
S M
SM
D001142:Aromatic-L-Amino-Acid Decarboxylases / Q000378:metabolism*; D004296:Dopa Decarboxylase / Q000378:metabolism*; D005583:Fourier Analysis; D007700:Kinetics; D007834:Lasers; D008433:Mathematics; D006005:Phosphorylases / Q000378:metabolism*
D006005:Phosphorylases; D004296:Dopa Decarboxylase; D001142:Aromatic-L-Amino-Acid Decarboxylases