Lanthanides as probes for calcium in biological systems
- 1 May 1979
- journal article
- research article
- Published by Cambridge University Press (CUP) in Quarterly Reviews of Biophysics
- Vol. 12 (2) , 181-209
- https://doi.org/10.1017/s0033583500002754
Abstract
Calcium ion plays an essential role in many biological processes. The environment about Ca2+may be probed by substitution of tripositive lanthanide ions, Ln3+. Ca2+proteins fall into two broad classes: those that are inhibited by Ln3+substitution and those that are not. It is suggested that although Ca2+undertakes a primarily structural role in the Ln3+non-inhibited proteins, Ca2+may be near the active site or participate in the mechanism of action of Ln3+inhibited proteins. Ca2+and Ln3+radii are similar; most Ln3+are slightly larger than Ca2+in complexes of the same coordination number, and substitution of Ln3+for Ca2+is accommodated by a slight decrease in bond distance or by an increase in coordination number. Luminescence from Tb3+has been demonstrated to be a sensitive environmental probe of Ca2+binding sites in proteins.Keywords
This publication has 107 references indexed in Scilit:
- Circularly polarized emission of terbium(III) substituted bovine cardiac troponin-CBiochemical and Biophysical Research Communications, 1976
- Interaction between calcium and ligand-binding sites of the purified acetylcholine receptor studied by use of a fluorescent lanthanideBiochemical and Biophysical Research Communications, 1976
- The location of the lanthanide ion binding site on bovine trypsinBiochemical and Biophysical Research Communications, 1975
- The amino acid sequence of bovine cardiac troponin-C. Comparison with rabbit skeletal troponin-CBiochemical and Biophysical Research Communications, 1975
- Homology of myosin light chains, troponin-C and parvalbumins deduced from comparison of their amino acid sequencesBiochemical and Biophysical Research Communications, 1974
- Binding of Ca2+ to normal and dicoumarol-induced prothrombinBiochemical and Biophysical Research Communications, 1973
- Aequorin: Its ionic specificityBiochemical and Biophysical Research Communications, 1972
- Cation requirements of isoleucyl-tRNA synthetase from EscherichiacoliBiochemical and Biophysical Research Communications, 1972
- Calcium carrier and the “high affinity calcium binding site” in mitochondriaBiochemical and Biophysical Research Communications, 1969
- Calcium metabolism in cardiac microsomes incubated with lanthanum ionBiochemical and Biophysical Research Communications, 1969