Regular ArticleComplementary Mössbauer and EPR Studies of Iron(III) in Diferric Human Serum Transferrin with Oxalate or Bicarbonate as Synergistic Anions
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Substitution of carbonate by non-physiological synergistic anion modulates the stability and iron release kinetics of serum transferrin
2023, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :The differences in the ability of iron-binding between the two lobes of transferrin [19,57–60] were ascribed to the differences in the second shell network formed by amino acid residues that are hydrogen-bonded to the main ligand [60]. It is emphasized that the replacement of one synergistic anion with another can cause the in-equivalency of metal-binding sites [30–32]. Particularly, the substitution of carbonate by oxalate has been established as a reliable assay to distinguish the site-specific binding in Tfs [30–32].
Human transferrin: An inorganic biochemistry perspective
2021, Coordination Chemistry ReviewsCitation Excerpt :For such spin states, dipolar interactions and strong spin–orbit coupling removes the ground-state degeneracy leading to splitting of the strongly coupled S = 5/2 Kramers doublets even in the absence of the external magnetic field, the so-called zero-field splitting (ZFS) [97–101]. Consequently, the characterization of the electronic and magnetic properties of high-spin d5 Fe(III) centers in metalloprotein has been predominantly obtained from independent or combined studies of EPR and Mössbauer spectroscopies [102–105]. X-ray absorption studies have also provided valuable and complementary information regarding the elucidation of metalloprotein Fe(III) centers [106–108].
The oxalate effect on release of iron from human serum transferrin explained
2004, Journal of Molecular BiologyCitation Excerpt :The inequivalency of the sites is accentuated by substitution of different metals or synergistic anions. In particular, as detailed previously14–17 oxalate has been a useful probe to identify site-specific binding preferences in hTF, LTF and oTF. Several observations highlight the importance of anion binding in the TF family; most obvious is that no metal, including Fe(III), can be tightly bound by TF in the absence of a suitable synergistic anion.
Many-Body Study of Iron(III)-Bound Human Serum Transferrin
2022, Journal of Physical Chemistry Letters