Mg²⁺ binding to parvalbumins studied by ²⁵Mg and ¹¹³Cd NMR spectroscopy

Metal-ion binding to parvalbumin. A 113Cd-n.m.r. study of the binding of different lanthanide ions

“…suppresses the broadening induced by 0.15equiv. of Gd3+ on resonance 1 and shifts this resonance to high field, as previously described for similar amounts of Mg2+ (Cave et al, 1979b(Cave et al, , 1982, showing that Mg2+ and Gd3+ compete for the same binding site and that the ratio in the binding constants, KGd/KMg, can be estimated to be between 100 and 1000.…”

Molecular Tuning of Ion Binding to Calcium Signaling Proteins

“…7-9 x 1 o" 8 (I3±2)XIO"°2 X IO" 6 2 X IO" 7 3 x io" 6 5 x io" 8 3 x io" 6 7 x io" 8 3-7 xio" 1 0 Reference Christensen, 1975Christensen, 1975Kauffman et al 1976Falke et al 1991Burger et al 1984Wang, 1985Burger et al 1984Wang, 1985Drabikowski et al 1982 Potter & Johnson, 1982* Potter & Johnson, 1982Potter & Johnson, 1982Potter & Johnson, 1982Moeschler et al 1980Cave et al 1979 Ionic strength. IT monovalent ion and Mg 2+ affinities enable a regulatory domain to remain in its inactive apo-conformation until a Ca 2+ signal appears.…”

“…In contrast to sites acting as Ca 2+ triggers, structural or buffering EF-hand sites may be required to bind a divalent cation even in the absence of a Ca 2+ signal, thus these sites often possess higher Mg 2+ affinities. For example, Table 6 indicates that parvalbumin and the C-terminal domains of calmodulin, skeletal troponin C, and cardiac troponin C each bind Mg 2+ tightly enough to yield significant physiological occupancy (K 1/2 < ~ i mM; Cave et al 1979;Drabikowski et al 1982;Potter & Johnson, 1982). These sites typically exhibit higher Ca 2+ affinities as well; in fact, they bind Ca 2+ with up to 20-fold greater specificity than the signaling sites, as quantitated by the ratio of macroscopic binding constants K Ca /K Mg (Table 6).…”

Vibrational spectra of hydrates of some metal(II) malonates

“…The metal malonates can act as inhibitors of matrix metalloproteinases, as well as like a model for ccarboxyglutamic acid [10]. Thus, cadmium(II) malonates are suitable models for examining the coordination of metalloproteins in saccharide-specific lectin concanavalin A [11] and parvalbumin [12,13].…”