1 publication

1 publication

Rare Earth Metal Ions as Probes of Calcium Binding Sites in Proteins: Neodynium Acceleration of the Activation of Trypsinogen

Birnbaum, E.R.; Darnall, D.W.

J. Biol. Chem. 1970, n/a

The rate of activation of the conversion of trypsinogen to trypsin has been found to be greatly accelerated by the neodymium(III) ion. The similarity of this process to the calcium(II) ion activation suggests that both metal ions bind at identical sites in trypsinogen. The rate of activation in the presence of the neodymium ion is much greater than that of the calcium ion, probably reflecting the increased stability constant of the neodymium-protein complex. In contrast to the calcium ion, however, neodymium(III) can be scrutinized by a variety of spectral and magnetic techniques which should reveal information concerning the calcium ion binding sites in proteins. Since the chemistry and the range of sires of the rare earth metal ions are so similar to that of the calcium ion, it is suggested that generally these ions should make good replacement ions for probing the calcium ion binding sites of proteins and enzymes.

Metal: Nd
Ligand type: Amino acid
Host protein: Trypsin
Anchoring strategy: Metal substitution
Optimization: ---
Max TON: <1
ee: ---
PDB: ---
Notes: PMID 5484822