Fe 3+ binding to ovotransferrin in the presence of α-amino acids
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, ISSN: 0167-4838, Vol: 1118, Issue: 3, Page: 313-317
1992
- 6Citations
- 6Captures
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Article Description
The ability of l -α-amino acids as synergistic anions for iron binding to ovotransferrin was investigated through electronic spectroscopy. Glycine and glutamic acid were found to form by far the most stable ternary Fe 3+ ovotransferrin-amino acid complexes. Less stable adducts were formed by amino acids with a hydroxy, amide or sulphur-containing group in the side chain, while the complexes with leucine, isoleucine, valine, lysine, arginine, tyrosine and tryptophan failed to form. Evidence is obtained that the synergistic effectiveness of the H 2 N-CH-COO − moiety is determined not only by the isoelectric point of the amino acid and the steric hindrance of its side chain, but a significant role is also played by interactions of the side chain itself with residues in the metal binding domains. Zn 2+, Cd 2+ and Co 2+ are found to bind to ovotransferrin in the presence of glycine. 113 Cd-NMR spectra on the Cd-derivative indicate that, according to the interlocking-sites model, the amino group of glycine directly binds to the metal ion.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/016748389290290T; http://dx.doi.org/10.1016/0167-4838(92)90290-t; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0026814574&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/1346572; http://linkinghub.elsevier.com/retrieve/pii/016748389290290T; http://api.elsevier.com/content/article/PII:016748389290290T?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:016748389290290T?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/016748389290290T; http://dx.doi.org/10.1016/0167-4838%2892%2990290-t; https://dx.doi.org/10.1016/0167-4838%2892%2990290-t
Elsevier BV
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