Perfluorodecanoic acid binding to hemoproteins: new insights from spectroscopic studies.

Perfluorodecanoic acid (PFDA), a representative of the perfluoroalkyl acids, poses a great threat to humans and animals via food and other potential sources. In this work, we determined the effects of PFDA binding to two hemoproteins, bovine hemoglobin (BHb) and myoglobin (Mb). Using fluorescence spectroscopy, we found that PFDA greatly enhanced the fluorescence intensity of both hemoproteins, while perfluorooctanoic acid (PFOA) and perfluoropentanoic acid (PFPA) have minimal effects on the fluorescence. UV-vis absorption (UV) spectroscopy showed that PFDA induced the unfolding of the hemoproteins accompanied by exposure of the heme pocket and facilitating the formation of hemichrome. Additionally, as shown by the circular dichroism (CD) data, PFDA altered the secondary structure of both BHb and Mb. This work elucidates the interaction mechanism of PFDA with two hemoproteins.