title: A deactivating conformational change induced by reduced nicotinamide-adenine dinucleotide phosphate in a Neurospora glutamate dehydrogenase.
abstract: Stopped-flow fluorescence techniques have been used to observe the formation of the binary comples of E-NADPH. At pH 7.5 there is a protein conformational change after the formation of the binary complex. This conformational change can be detected by a decrease in the fluorescence intensity of the complex at 350 nm and by an increase in its fluorescence intensity at 450 nm.
mesh_terms: D005453:Fluorescence; D005969:Glutamate Dehydrogenase; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009249:NADP; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*; D011487:Protein Conformation
chemical_list: D009249:NADP; D005969:Glutamate Dehydrogenase