Toxic effects of copper (II) ions on bovine hemoglobin. Issue 2 (7th February 2018)

• Record Type: Journal Article
• Authors: Li, Sha; Shang, Hongyuan; Liu, Fasheng; Ma, Min; Zhang, Aiping
• Is Part Of: Spectroscopy letters. Volume 51:Issue 2(2018)
• Page Start: 67
• Page End: 73
• Publication Date: 2018-02-07
• Subjects: Bovine hemoglobin (BHb) -- copper ions (II) -- spectroscopic methods -- toxic effect; Spectrum analysis -- Periodicals; 543.5
• DOI: 10.1080/00387010.2017.1335754
• Languages: English
• ISSNs: 0038-7010

Abstract

ABSTRACT: In this paper, the toxic influence of copper ions (II) on bovine hemoglobin was investigated by the combination of ultraviolet-visible absorption, fluorescence, time-resolved fluorescence, synchronous fluorescence, and circular dichroism spectra. Driven by hydrophobic and electrostatic forces, copper ions (II) could interact with bovine hemoglobin to form bovine hemoglobin-copper ions (II) complex with one binding site. The binding constant ( K ) was 1.57 × 10 4, 1.89 × 10 4 and 2.11 × 10 4 L/mol at 298, 304, and 310 K, respectively. The binding distance ( r ) was 4.24 nm. Fluorescence and time-resolved fluorescence spectra showed that bovine hemoglobin quenched by copper ions (II) was a static quenching process. Results of synchronous fluorescence spectra revealed that the microenvironment and the conformation of bovine hemoglobin were changed during the binding reaction. Data of circular dichroism spectra suggested that with the increasing concentration of copper ions (II), the secondary structure of bovine hemoglobin underwent a decrease in α -helix and alteration in backbone microenvironment. Copper ions (II) was thus evidenced to have a certain toxic effect on physical bodies.