Journal
JOURNAL OF HAZARDOUS MATERIALS
Volume 307, Issue -, Pages 281-293Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jhazmat.2015.12.029
Keywords
Hemoglobin; Metal-protein binding; Structural and functional alterations
Categories
Funding
- BARC, Government of India
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Due to increasing use of lanthanides/actinides in nuclear and civil applications, understanding the impact of these metal ions on human health and environment is a growing concern. Hemoglobin (Hb), which occurs in all the kingdom of living organism, is the most abundant protein in human blood. In present study, effect of lanthanides and actinides [thorium: Th(IV), uranium: U(VI), lanthanum: La(III), cerium: Ce(III) and (IV)] on the structure and function of Hb has been investigated. Results showed that these metal ions, except Ce(IV) interacted with carbonyl and amide groups of Hb, which resulted in the loss of its alpha helix conformation. However, beyond 75 mu M, these ions affected heme moiety. Metal-heme interaction was found to affect oxygen-binding of Hb, which seems to be governed by their closeness with the charge to-ionic-radius ratio of iron(III). Consistently, Ce(IV) being closest to iron(Ill), exhibited a greater effect on heme. Binding constant and binding stoichiometry of Th(IV) were higher than that of U(VI). Experiments using aquatic midge Chironomus (possessing human homologous Hb) and human blood, further validated metal-Hb interaction and associated toxicity. Thus, present study provides a biochemical basis to understand the actinide/lanthanide-induced interference in heme, which may have significant implications for the medical and environmental management of lanthanides/actinides toxicity. (C) 2015 Elsevier B.V. All rights reserved.
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