The pH-induced release of iron from transferrin investigated with a continuum electrostatic model

Biophysical Journal
D A Lee, J M Goodfellow

Abstract

A reduction in pH induces the release of iron from transferrin in a process that involves a conformational change in the protein from a closed to an open form. Experimental evidence suggests that there must be changes in the protonation states of certain, as yet not clearly identified, residues in the protein accompanying this conformational change. Such changes in protonation states of residues and the consequent changes in electrostatic interactions are assumed to play a large part in the mechanism of release of iron from transferrin. Using the x-ray crystal structures of human ferri- and apo-lactoferrin, we calculated the pKa values of the titratable residues in both the closed (iron-loaded) and open (iron-free) conformations with a continuum electrostatic model. With the knowledge of a residue's pKa value, its most probable protonation state at any specified pH may be determined. The preliminary results presented here are in good agreement with the experimental observation that the binding of ferric iron and the synergistic anion bicarbonate/carbonate results in the release of approximately three H+ ions. It is suggested that the release of these three H+ ions may be accounted for, in most part, by the deprotonation of the ...Continue Reading

References

Nov 1, 1992·Biophysical Journal·M ZachariasJ A McCammon
Jul 1, 1991·Proceedings of the National Academy of Sciences of the United States of America·P BerozaG Feher
Nov 15, 1989·Archives of Biochemistry and Biophysics·R VíghI Simon
Apr 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·B F AndersonE N Baker
Jun 1, 1971·Biopolymers·M Y Rosseneu-MotreffH Peeters
Mar 1, 1980·Archives of Biochemistry and Biophysics·M H Gelb, D C Harris
Nov 30, 1995·Biochimica Et Biophysica Acta·Z M Qian, P L Tang
Jun 15, 1995·European Journal of Biochemistry·J M el Hage Chahine, R Pakdaman
Feb 5, 1993·Journal of Molecular Biology·J G GrossmannS S Hasnain
Jan 1, 1996·Physiological Reviews·D M de SilvaJ Kaplan
Apr 11, 1997·Journal of Molecular Biology·H X Zhou, M Vijayakumar
Jul 1, 1997·Protein Engineering·J Warwicker
Sep 24, 1963·Biochimica Et Biophysica Acta·R AASAP SALTMAN

❮ Previous
Next ❯

Citations

Oct 28, 1998·Proceedings of the National Academy of Sciences of the United States of America·A Pekosz, R A Lamb
Aug 12, 2009·Vox Sanguinis·A ShanderL T Goodnough
Nov 27, 2015·Physical Chemistry Chemical Physics : PCCP·Arpan BhattacharyaTushar Kanti Mukherjee
May 23, 2014·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Sandeep KumarRajesh Kumar
May 1, 2020·Dalton Transactions : an International Journal of Inorganic Chemistry·Karthika J KadasseryDavid C Lacy
Jun 29, 2018·Frontiers in Immunology·Ghanshyam Swarup, Zuberwasim Sayyad
Aug 19, 2009·The Journal of Physical Chemistry. B·Rajesh Kumar, A Grant Mauk
Nov 30, 2011·The Journal of Physical Chemistry. B·Jagannath MondalArun Yethiraj
Mar 1, 2012·The Journal of Physical Chemistry. B·Rajesh Kumar, A Grant Mauk

❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Cell Wall Structure (ASM)

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.