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פותח על ידי קלירמאש פתרונות בע"מ -
Fluorescence decay time measurements of Eu3+-ATP-enzyme complexes. Replacement of the metal hydration water by active site ligands.
Year:
1983
Source of publication :
Journal of Biological Chemistry
Authors :
גוטמן, מריו
;
.
Volume :
258
Co-Authors:
Gutman, M.
Levy, M.A.
Facilitators :
From page:
12132
To page:
12134
(
Total pages:
3
)
Abstract:
Measurements of the fluorescent lifetimes of the rare earth metal Eu3+ in varying mole fractions of H2O/D2O were used to determine the hydration of the metal in the presence of ATP and/or hexokinase or chloroplast reversible ATPase. The number of water molecules coordinated to the metal in Eu3+-ATP was estimated to be 2.6; when this complex is bound to hexokinase, 1 water molecule is displaced. Upon binding to chloroplast reversible ATPase, the metal coordinates 1 water molecule while the Eu3+-ATP complex does not retain any associated solvent. These numbers are in contrast to the 9 solvent molecules coordinated to the naked metal ion. These results are discussed in reference to mechanistic and structural considerations of the two enzymes.
Note:
Related Files :
Adenosinetriphosphatase
adenosine triphosphate
Chloroplasts
Kinetics
metabolism
plant
Plants
protein binding
עוד תגיות
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More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
30344
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:53
Scientific Publication
Fluorescence decay time measurements of Eu3+-ATP-enzyme complexes. Replacement of the metal hydration water by active site ligands.
258
Gutman, M.
Levy, M.A.
Fluorescence decay time measurements of Eu3+-ATP-enzyme complexes. Replacement of the metal hydration water by active site ligands.
Measurements of the fluorescent lifetimes of the rare earth metal Eu3+ in varying mole fractions of H2O/D2O were used to determine the hydration of the metal in the presence of ATP and/or hexokinase or chloroplast reversible ATPase. The number of water molecules coordinated to the metal in Eu3+-ATP was estimated to be 2.6; when this complex is bound to hexokinase, 1 water molecule is displaced. Upon binding to chloroplast reversible ATPase, the metal coordinates 1 water molecule while the Eu3+-ATP complex does not retain any associated solvent. These numbers are in contrast to the 9 solvent molecules coordinated to the naked metal ion. These results are discussed in reference to mechanistic and structural considerations of the two enzymes.
Scientific Publication
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