[Fluorescence spectroscopic study of interaction between Fe-protoporphyrin in myoglobin and Cu(II) ions].
In this paper, the interaction between Cu(II) ions and Fe-protoporphyrin in horse-heart myoglobin (FePP-Mb) was studied. As a result, some of the Fe(II) ions in FePP-Mb were found to be replaced by Cu(II) ions forming CuPP-Mb, by adding Cu(II) ions into the myoglobin solution. The interaction became stronger when adding more Cu(II) ions into the myoglobin solution. By studying the metal ions' interaction with myoglobin proteins as macromolecules and discussing the interaction mechanism, this work provides a theoretical basis for the further study of hazardous metal ions' interaction with the human body and its mechanism. The fluorescence spectroscopic method used in this study has higher sensitivity than the ordinary UV and CD methods.
Feng
Yu-ying
YY
Analysis and Testing Center, Nanjing Normal University, Nanjing 210097, China.
Yang
Hui
H
Gu
Xiao-tian
XT
Jiang
Hui-jun
HJ
Lu
Tian-hong
TH
D000818:Animals; D003300:Copper / Q000737:chemistry*; D004347:Drug Interactions; D006736:Horses; D007501:Iron / Q000737:chemistry*; D009206:Myocardium / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry*; D011524:Protoporphyrins / Q000737:chemistry*
D009211:Myoglobin; D011524:Protoporphyrins; C448299:iron protoporphyrin IX; D003300:Copper; D007501:Iron