Fluorescence resonance energy transfer studies on the proximity between lysine-107 and cysteine-239 in rabbit muscle aldolase.
Spatial relationships between Lys-107, which binds the C-6 phosphate group of the substrate, and fast-reacting Cys-239, located outside the active site of rabbit muscle aldolase, were studied by means of resonance energy transfer. The Lys-107 residue was covalently linked to pyridoxal phosphate (fluorescence donor) and the Cys-239 residue was modified by 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (fluorescence acceptor). The energy transfer between donor and acceptor has been demonstrated. The steady-state and the lifetime measurements indicate that in solution the distance between Lys-107 and Cys-239 in the aldolase molecule is 12.4 A assuming chi 2 = 2/3.
D009327:4-Chloro-7-nitrobenzofurazan / Q000378:metabolism; D000818:Animals; D003545:Cysteine; D004735:Energy Transfer; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D008239:Lysine; D009132:Muscles / Q000201:enzymology; D011485:Protein Binding; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000378:metabolism; D011733:Pyridoxamine / Q000031:analogs & derivatives / Q000378:metabolism; D011817:Rabbits; D013050:Spectrometry, Fluorescence / Q000379:methods
D011732:Pyridoxal Phosphate; D011733:Pyridoxamine; D005634:Fructose-Bisphosphate Aldolase; D009327:4-Chloro-7-nitrobenzofurazan; D008239:Lysine; D003545:Cysteine; C010627:pyridoxamine phosphate