title: Spectroscopic investigation on the toxic interactions of Ni2+ with bovine hemoglobin.
abstract: The toxic interaction between Ni(2+) and bovine hemoglobin (BHb) was investigated using fluorescence spectroscopy, synchronous fluorescence spectroscopy, ultraviolet-visible (UV-vis) absorption spectroscopy and circular dichroism spectroscopy (CD) under simulated physiological conditions. The experimental results showed that both dynamic and static quenching occurred simultaneously when Ni(2+) quenched the fluorescence of BHb. The binding site number n, apparent binding constant K(a) and corresponding thermodynamic parameters were measured at different temperatures. There was formation of Ni-BHb complex, but the binding between Ni(2+) and BHb was not strong. The process of the formation of Ni-BHb complex was a spontaneous interaction procedure in which electrostatic interaction played a major role. In addition, UV-vis and CD results showed that the addition of Ni(2+) changed the conformation of BHb.
authors.affiliation: School of Environmental Science and Engineering, Shandong University, 27# Shanda South Road, Jinan 250100, PR China.
authors.forename: Li
authors.initials: L
authors.lastname: Wang
authors.forename: Rutao
authors.initials: R
authors.lastname: Liu
authors.forename: Zhenxing
authors.initials: Z
authors.lastname: Chi
authors.forename: Bingjun
authors.initials: B
authors.lastname: Yang
authors.forename: Pengjun
authors.initials: P
authors.lastname: Zhang
authors.forename: Meijie
authors.initials: M
authors.lastname: Wang
mesh_terms: D000818:Animals; D002413:Cations, Divalent / Q000378:metabolism; D002417:Cattle; D002942:Circular Dichroism; D006454:Hemoglobins / Q000378:metabolism*; D009532:Nickel / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
chemical_list: D002413:Cations, Divalent; D006454:Hemoglobins; D009532:Nickel