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Interaction of vanadium(IV) with human serum apo-transferrin.

Abstract：

:The interaction of V(IV)O-salts as well as of a few V(IV)O(carrier)n complexes with human serum transferrin (hTF) is studied focusing on the determination of the nature and stoichiometry of the binding of V(IV)O(2+) to hTF, as well as whether the conformation of hTF upon binding to V(IV)O(2+) or to its complexes is changed. Circular dichroism (CD) spectra measured for solutions containing V(IV)O(2+) and apo-hTF, and V(IV)O-maltol and apo-hTF, clearly indicate that hTF-V(IV)O-maltol ternary species form with a V(IV)O:maltol stoichiometry of 1:1. For V(IV)O salts and several V(IV)O(carrier)n complexes (carrier ligand=maltolato, dhp, picolinato and dipicolinato) (Hdhp=1,2-dimethyl-3-hydroxy-4-pyridinone) the maximum number of V(IV)O(2+) bound per mole of hTF is determined to be ~2 or lower in all cases. The binding of V(IV)O to apo-hTF most certainly involves several amino acid residues of the Fe-binding site, and as concluded by urea gel electrophoresis experiments, the formation of (V(IV)O)2hTF species may occur with the closing of the hTF conformation as is the case in (Fe(III))2hTF, which is an essential feature for the transferrin receptor recognition.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

Mehtab S,Gonçalves G,Roy S,Tomaz AI,Santos-Silva T,Santos MF,Romão MJ,Jakusch T,Kiss T,Pessoa JC

doi

10.1016/j.jinorgbio.2012.12.020

subject

Has Abstract

pub_date

2013-04-01 00:00:00

pages

187-95

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(13)00014-7

journal_volume

121

pub_type

杂志文章

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