Resolution of the two metal binding sites of human serum transferrin by low-temperature excitation of bound europium(III)

Biochemistry ◽  
1982 ◽  
Vol 21 (21) ◽  
pp. 5269-5272 ◽  
Author(s):  
Patricia B. O'Hara ◽  
Richard Bersohn
Keyword(s):  
Low Temperature ◽  
Human Serum ◽  
Metal Binding ◽  
Binding Sites ◽  
Serum Transferrin ◽  
Human Serum Transferrin ◽  
Metal Binding Sites

scholarly journals The distribution of iron between the metal-binding sites of transferrin human serum

1980 ◽  
Vol 185 (2) ◽  
pp. 483-488 ◽  
Author(s):  
J Williams ◽  
K Moreton
Keyword(s):  
Human Serum ◽  
Metal Binding ◽  
Binding Sites ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Iron Binding ◽  
Metal Binding Sites ◽  
Fresh Serum ◽  
Marked Preference ◽  
Terminal Site

The Makey & Seal [(1976) Biochim. Biophys. Acta 453, 250-256] method of polyacrylamide-gel electrophoresis in buffer containing 6 M-urea was used to determine the distribution of iron between the N-terminal and C-terminal iron-binding sites of transferrin in human serum. In fresh serum the two sites are unequally occupied; there is preferential occupation of the N-terminal site. On incubation of the serum at 37 degrees C the preference of iron for the N-terminal site becomes more marked. On storage of serum at −15 degrees C the iron distribution changes so that there is a marked preference for the C-terminal site. Dialysis of serum against buffer at pH 7.4 also causes iron to be bound much more strongly by the C-terminal than by the N-terminal site. The original preference for the N-terminal site can be resroted to the dialysed serum by addition of the diffusible fraction.

scholarly journals Periodate Modification of Human Serum Transferrin Fe(III)-binding Sites.

1995 ◽  
Vol 270 (21) ◽  
pp. 12404-12410 ◽  
Author(s):  
David C. Ross ◽  
Timothy J. Egan ◽  
Langley R. Purves
Keyword(s):  
Human Serum ◽  
Binding Sites ◽  
Serum Transferrin ◽  
Human Serum Transferrin

Effects of Mutations of Aspartic Acid 63 on the Metal-Binding Properties of the Recombinant N-Lobe of Human Serum Transferrin†

Biochemistry ◽  
1997 ◽  
Vol 36 (18) ◽  
pp. 5522-5528 ◽  
Author(s):  
Qing-Yu He ◽  
Anne B. Mason ◽  
Robert C. Woodworth ◽  
Beatrice M. Tam ◽  
Toby Wadsworth ◽  
...  
Keyword(s):  
Human Serum ◽  
Aspartic Acid ◽  
Metal Binding ◽  
Serum Transferrin ◽  
Binding Properties ◽  
Human Serum Transferrin

A Density Functional Theory Study of the Iron-Binding Site of Human Serum Transferrin

2004 ◽  
Vol 57 (12) ◽  
pp. 1219 ◽  
Author(s):  
David Rinaldo ◽  
Martin J. Field
Keyword(s):  
Human Serum ◽  
Binding Site ◽  
Conformational Changes ◽  
Metal Binding ◽  
Density Functional ◽  
Release Mechanism ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Iron Release ◽  
Human Serum Transferrin

Human serum transferrin binds ferric ions with high affinity in the blood stream and releases them into cells by a process involving receptor-mediated endocytosis and a decrease in pH. The iron-release mechanism is unclear but protonation events and conformational changes are known to be important. In this study, we investigate properties of the iron-binding site theoretically. Our results suggest that an equatorial histidine could be in its histidinate form when bound to iron at neutral and high pH and that protonation of an axial tyrosine is a key event in iron release. Support for this mechanism from other metal-binding enzymes is also presented.

“Anion clamp” allows flexible protein to impose coordination geometry on metal ions

2015 ◽  
Vol 51 (37) ◽  
pp. 7867-7870 ◽  
Author(s):  
Minji Wang ◽  
Tsz Pui Lai ◽  
Li Wang ◽  
Hongmin Zhang ◽  
Nan Yang ◽  
...  
Keyword(s):  
Metal Ions ◽  
Human Serum ◽  
Metal Binding ◽  
Binding Pocket ◽  
Serum Transferrin ◽  
Coordination Geometry ◽  
Human Serum Transferrin ◽  
Lanthanide Ion ◽  
X Ray ◽  
Flexible Protein

X-ray crystal structures of human serum transferrin (77 kDa) with YbIII or FeIII bound to the C-lobe and malonate as the synergistic anion show that the large YbIII ion causes the expansion of the metal binding pocket while octahedral metal coordination geometry is preserved, an unusual geometry for a lanthanide ion.

scholarly journals Exploring the Fe(III) binding sites of human serum transferrin with EPR at 275 GHz

2014 ◽  
Vol 20 (3) ◽  
pp. 487-496 ◽  
Author(s):  
Guinevere Mathies ◽  
Peter Gast ◽  
N. Dennis Chasteen ◽  
Ashley N. Luck ◽  
Anne B. Mason ◽  
...  
Keyword(s):  
Human Serum ◽  
Binding Sites ◽  
Serum Transferrin ◽  
Human Serum Transferrin
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