NDLI: Unusual features for zirconium(IV) binding to human serum transferrin

Content Provider	Springer Nature Link
Author	Zhong, Weiqing Parkinson, John A. Guo, Maolin Sadler, Peter J.
Copyright Year	2002
Abstract	Human serum apotransferrin (hTF) binds to Zr(IV) slowly in the presence of nitrilotriacetate (NTA), citrate or ethylenediaminetetraacetate (EDTA) as donor ligands. For Zr(NTA)2 2– as donor, equilibrium was reached in ca. 2 h (pH 7.4, 298 K, 10 mM Hepes, 5 mM bicarbonate) and full loading of the N- and C-lobe sites was achievable to give Zr2-hTF. 13C NMR data suggest that carbonate can bind as a synergistic anion. 1H and 2D [1H,13C] (using ε-[13C]Met-hTF) NMR studies show that there is little lobe-selectively in the order of Zr(IV) uptake. Fe(III) displaced Zr(IV) from the C-lobe of Zr2-hTF first, followed by the N-lobe. However, in the presence of a large excess of NTA, Zr(IV) binds to the N-lobe of holo-hTF (Fe2-hTF) first followed by the C-lobe. The 1H and 13C NMR chemical shift changes for ε-[13CH3] of Met464, which is close to the C-lobe site, are quite distinct from those observed previously for Al(III), Fe(III), Ti(IV), Ga(III) and Bi(III) binding to hTF, suggesting that Zr(IV) binding may not induce lobe closure [as observed previously for Hf(IV)]. This may affect receptor recognition and play a role in the different biological behaviour of Zr(IV) compared to Ti(IV).
Starting Page	589
Ending Page	599
Page Count	11
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	7
Issue Number	6
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2002-02-15
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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