Fluorescence resonance energy transfer studies on the proximity between lysine-107 and cysteine-239 in rabbit muscle aldolase.

Abstract

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.

Cite this paper

@article{Dobryszycki1988FluorescenceRE, title={Fluorescence resonance energy transfer studies on the proximity between lysine-107 and cysteine-239 in rabbit muscle aldolase.}, author={Piotr Dobryszycki and Monika Kochman}, journal={Biochimica et biophysica acta}, year={1988}, volume={956 3}, pages={217-23} }