Revealing the complexity of distinct manganese species-protein interactions through multi-spectroscopy.

The effect of manganese (Mn) on protein conformation is closely related to its chemical species. To further realize the behavior of different species of Mn in vivo, this study is designed to analyze the separate and simultaneous interactions of Mn(ii) and Mn(iii) with bovine serum albumin (BSA) using multi-spectroscopy. The results demonstrated that the interaction of Mn(ii) or Mn(iii) with BSA is a process of static quenching and Mn(iii) formed a more stable complex. The binding constants and thermodynamic constants indicated that a 1:1 complex was formed between Mn(ii)/Mn(iii) and BSA through a moderate binding force, and hydrophobic interaction played an important role in the binding. UV-Vis spectroscopy, synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy results revealed that the conformation changes in BSA induced by Mn(ii)/Mn(iii) binding. The results of the ternary systems suggested that both Mn species interfered the interaction of the other with BSA. The conformation of BSA may change more to adapt to the simultaneous binding to Mn (ii) and Mn (iii) when two Mn species coexist.