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The study of exchange between free and metal-bound ligands by NMR methods is discussed with reference to differentiation between unimolecular dissociation of the metal-bound complex and biomolecular exchange of metal ion between two ligands. This is applied to exchange of ATP4- between the free and Mg2(+)-bound states and problems of interpretation in the presence of a strong kinetic salt effect are discussed. Contrary to a previous report, exchange is inferred to occur mainly via unimolecular dissociation of MgATP2- over a range of temperatures, concentrations, and pH values, which include those expected in vivo. For the model system Mg2(+)-tripolyphosphate, an activation energy of 52 +/- 5 kJ.mol-1, inferred to be that for dissociation of MgTPPH2-, is found for the exchange process.
E O Bishop, and
R Miles, and
B E Smith
February 1986,
Biochemical and biophysical research communications,
E O Bishop, and
R Miles, and
B E Smith
August 1984,
Journal of inorganic biochemistry,
E O Bishop, and
R Miles, and
B E Smith
February 1989,
FEBS letters,
E O Bishop, and
R Miles, and
B E Smith
August 1990,
Biochimica et biophysica acta,
E O Bishop, and
R Miles, and
B E Smith
October 1992,
The International journal of biochemistry,
E O Bishop, and
R Miles, and
B E Smith
August 1996,
The Journal of biological chemistry,
E O Bishop, and
R Miles, and
B E Smith
February 1977,
Nucleic acids research,
E O Bishop, and
R Miles, and
B E Smith
January 1980,
Zeitschrift fur Naturforschung. Section C, Biosciences,
E O Bishop, and
R Miles, and
B E Smith
February 1982,
Biochimica et biophysica acta,
E O Bishop, and
R Miles, and
B E Smith
September 1982,
Biochemical and biophysical research communications,
