Structural studies on metal-serum albumin. IV. The interaction of Zn(II), Cd(II) and Hg(II) with HSA and BSA

• Published in: Biophysical chemistry Vol. 42; no. 2; pp. 201 - 211
• Main Authors: Yongqia, Zhou, Xuying, Hu, Chao, Dou, Hong, Liu, Sheyi, Wang, Panwen, Shen
• Format: Journal Article
• Language: English
• Published: London Elsevier B.V 01.02.1992; Amsterdam Elsevier; New York, NY
• Subjects: Animals; Binding Sites; Biological and medical sciences; Cadmium - metabolism; Cations, Divalent; Cattle; Fundamental and applied biological sciences. Psychology; Humans; Interactions. Associations; Intermolecular phenomena; Mercury - metabolism; Molecular biophysics; Optical electronegativity; Serum albumin; Serum Albumin - metabolism; Serum Albumin, Bovine - metabolism; Spectrophotometry, Ultraviolet; UV spectrum; XPS spectrum; Zinc - metabolism; Zinc group metal; Serum albumin; Zinc group metal; XPS spectrum; UV spectrum; Optical electronegativity; Metal complex; Binding site; Ultraviolet spectrometry; Divalent cation; X ray spectrum
• ISSN: 0301-4622; 1873-4200
• DOI: 10.1016/0301-4622(92)85010-2

There have been no detailed and reliable studies on the environment and configuration of Zn(II), Cd(II) and Hg(II) in the metal centers of human serum albumin and bovine serum albumin to date. In this paper the authentic evidence for the involvement of the cystinyl sulfur atoms in the ligation to the zinc group ions has been obtained from the X-ray photoelectron spectra. The belief that each of the zinc group ions possesses several similar binding sites in human- and bovine serum albumin and is bound to the deprotonated thiol group (-RS −) of the cysteinyl residues to form tetrahedral and linear metal centers has been further confirmed by the treatment of ligand to metal charge transfer data with Jorgensen's method. According to these results, we have inferred that these binding sites may be located at the seventeen disuifide bridges, most likely at the seven pairs of adjacent disulfide bridges between positions 75 and 567, in the serum albumins.