HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Gutman, M. Articles by Levy, M. A. Search for Related Content PubMed PubMed Citation Articles by Gutman, M. Articles by Levy, M. A. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 258, Issue 20, 12132-12134, 10, 1983

Fluorescence decay time measurements of Eu3+-ATP-enzyme complexes. Replacement of the metal hydration water by active site ligands

M Gutman and MA Levy

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.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?