Comparative study of glutamine synthetase bound lanthanide(III) ions using NMR relaxation and lanthanide(III) luminescence techniques
- 26 February 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 24 (5), 1221-1226
- https://doi.org/10.1021/bi00326a025
Abstract
Changes in the intrinsic fluorescence intensity of glutamine synthetase induced by lanthanide(III) ion binding demonstrate the existence of 3 types of sites for these ions. The sites are populated sequentially during titrations of the enzyme, and the first 2 have a stoichiometry of 1/enzyme subunit. The number of water molecules coordinated to Eu(III) bound to the 1st site was determined by luminescence lifetime techniques to be 4.1 .+-. 0.5. The hydration of Gd(III) bound to the same site was studied by magnetic field dependent water proton longitudinal relaxation rate measurements, and by water proton and deuteron relaxation measurements of 1 sample at single magnetic fields. The magnetic resonance techniques also yield a value of 4 for the hydration number.This publication has 6 references indexed in Scilit:
- Mn–Mn interaction in adenylylated and unadenylylated glutamine synthetaseBiochemical and Biophysical Research Communications, 1984
- Identification of the six ligands to manganese(II) in transition-state-analog complexes of creatine kinase: oxygen-17 superhyperfine coupling from selectively labeled ligandsBiochemistry, 1980
- Lanthanide ion probes of structure in biology. Laser-induced luminescence decay constants provide a direct measure of the number of metal-coordinated water moleculesJournal of the American Chemical Society, 1979
- A novel approach to water proton relaxation in paramagnetic ion-macromolecule complexesBiochemistry, 1977
- Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli W). I. Temperature and frequency dependent nuclear magnetic resonance studiesBiochemistry, 1976
- Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli W). II. Electron paramagnetic resonance and nuclear magnetic resonance studies of enzyme-bound manganese(II) with substrates and a potential transition-state analogue, methionine sulfoximineBiochemistry, 1976