Interaction between lanthanum ion and horseradish peroxidase in vitro.

The interaction between lanthanum ion (La(3+)) and horseradish peroxidase (HRP) in vitro was investigated using a combination of biophysical and biochemical methods. When the molar ratio of La(3+) and HRP is low, it was found that the interaction between La(3+) and HRP mainly depends on the electrostatic attraction, van der waals force and hydrogen bond etc. Thus, the interaction is weak and the La-HRP complex cannot be formed in vitro. As expected, the interaction can change the conformation of HRP molecule, leading to the increase in the non-planarity of the porphyrin ring in the heme group of HRP molecule, and then in the exposure degree of the active center, Fe(III) of the porphyrin ring of HRP molecule. Therefore, the catalytic activity of HRP for the H(2)O(2) reduction is improved. When the molar ratio of La(3+) and HRP is high, La(3+) can strongly coordinate with O and/or N in the amide group of the polypeptide chain of HRP molecule, forming the La-HRP complex. The formation of the La-HRP complex causes the change in the conformation of HRP molecule, leading to the decrease in the non-planarity of the porphyrin ring in the heme group of HRP molecule, and then in the exposure degree of the active center, Fe(III) of the porphyrin ring of HRP molecule. Thus, the catalytic activity of HRP for the H(2)O(2) reduction is decreased comparing with that of HRP in the absence of La(3+). The results can provide some references for understanding the interaction mechanism between trace elements ions and peroxidase in living organisms. 2009 Elsevier Masson SAS. All rights reserved.