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The monovalent cation site of pyruvate kinase and other enzymes: NMR investigations

Journal Article · · Fed. Proc.; (United States)
OSTI ID:5724148
Several monovalent cations have ideal physical properties for investigation of their interactions with biomacromolecules by NMR techniques. /sup 7/Li/sup +/, /sup 14/NH/sub 4//sup +/ and /sup 133/Cs/sup +/ have high natural abundance, and enriched samples of /sup 6/Li/sup +/ and /sup 15/NH/sub 4//sup +/ are easily obtained. All of these nuclei share the common property of having narrow line widths, thereby providing high sensitivity for NMR experiments. Numerous /sup 23/Na/sup +/ NMR studies have been reported but /sup 39/K/sup +/, /sup 85/Rb/sup +/, and /sup 87/Rb/sup +/ have not been studied extensively because these nuclei have low sensitivity and broad line widths. Recently NMR studies of monovalent cations have been extended to explore the monovalent cation sites of enzymes activated by such cations. With pyruvate kinase we determined that the extent of activation elicited by monovalent cations correlated well with the distance between the monovalent and divalent cations (structural site) sites. Those ions that were the best activators were closest to the M/sup 2 +/ site. In the course of this investigation we developed a general method to determine correlation times for dipolar relaxation between monovalent cation sites and paramagnetic centers on enzymes, and we have extended this work to other enzymes that are activated by monovalent cations.
Research Organization:
Pennsylvania State Univ., University Park
OSTI ID:
5724148
Journal Information:
Fed. Proc.; (United States), Journal Name: Fed. Proc.; (United States) Vol. 41:13; ISSN FEPRA
Country of Publication:
United States
Language:
English

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