Studies on plant calmodulin and its interaction with antagonist W-7 by Ln(3+) luminescence probes

Abstract

Plant calmodulin (CaM) has been extracted from cauliflower, and the purified CaM has been identified with the activation of NAD kinase (NADK) and the inhibition effect of CaM antagonist W-7. CaM's intrinsic fluorescence and Tb3+ fluorescence showed that there was one tyrosine residue and four metal-binding sites in cauliflower CaM. Based on Forster-type nonradiative energy theory, the distances of Tyr --> site III, IV have been determined, and these are 1.23 nm (Tyr --> site III ) and 1.18 nm(Tyr --> site IV). The Eu3+ and Tb3+ fluorescence probes showed that the combination of CaM with W-7 resulted in significant change on CaM's conformation, but did not affect coordination environment of metal-binding sites