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Redox properties of human transferrin bound to its receptor.

Publication ,  Journal Article
Dhungana, S; Taboy, CH; Zak, O; Larvie, M; Crumbliss, AL; Aisen, P
Published in: Biochemistry
January 2004

Virtually all organisms require iron, and iron-dependent cells of vertebrates (and some more ancient species) depend on the Fe(3+)-binding protein of the circulation, transferrin, to meet their needs. In its iron-donating cycle, transferrin is first captured by the transferrin receptor on the cell membrane, and then internalized to a proton-pumping endosome where iron is released. Iron exits the endosome to enter the cytoplasm via the ferrous iron transporter DMT1, a molecule that accepts only Fe(2+), but the reduction potential of ferric iron in free transferrin at endosomal pH (approximately 5.6) is below -500 mV, too low for reduction by physiological agents such as the reduced pyridine nucleotides with reduction potentials of -284 mV. We now show that in its complex with the transferrin receptor, which persists throughout the transferrin-to-cell cycle of iron uptake, the potential is raised by more than 200 mV. Reductive release of iron from transferrin, which binds Fe(2+) very weakly, is therefore physiologically feasible, a further indication that the transferrin receptor is more than a passive conveyor of transferrin and its iron.

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Published In

Biochemistry

DOI

EISSN

1520-4995

ISSN

0006-2960

Publication Date

January 2004

Volume

43

Issue

1

Start / End Page

205 / 209

Related Subject Headings

  • Transferrin
  • Thermodynamics
  • Receptors, Transferrin
  • Protein Binding
  • Peptide Fragments
  • Oxidation-Reduction
  • Kinetics
  • Humans
  • Ferrous Compounds
  • Ferric Compounds
 

Citation

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Dhungana, S., Taboy, C. H., Zak, O., Larvie, M., Crumbliss, A. L., & Aisen, P. (2004). Redox properties of human transferrin bound to its receptor. Biochemistry, 43(1), 205–209. https://doi.org/10.1021/bi0353631
Dhungana, Suraj, Céline H. Taboy, Olga Zak, Mykol Larvie, Alvin L. Crumbliss, and Philip Aisen. “Redox properties of human transferrin bound to its receptor.Biochemistry 43, no. 1 (January 2004): 205–9. https://doi.org/10.1021/bi0353631.
Dhungana S, Taboy CH, Zak O, Larvie M, Crumbliss AL, Aisen P. Redox properties of human transferrin bound to its receptor. Biochemistry. 2004 Jan;43(1):205–9.
Dhungana, Suraj, et al. “Redox properties of human transferrin bound to its receptor.Biochemistry, vol. 43, no. 1, Jan. 2004, pp. 205–09. Epmc, doi:10.1021/bi0353631.
Dhungana S, Taboy CH, Zak O, Larvie M, Crumbliss AL, Aisen P. Redox properties of human transferrin bound to its receptor. Biochemistry. 2004 Jan;43(1):205–209.
Journal cover image

Published In

Biochemistry

DOI

EISSN

1520-4995

ISSN

0006-2960

Publication Date

January 2004

Volume

43

Issue

1

Start / End Page

205 / 209

Related Subject Headings

  • Transferrin
  • Thermodynamics
  • Receptors, Transferrin
  • Protein Binding
  • Peptide Fragments
  • Oxidation-Reduction
  • Kinetics
  • Humans
  • Ferrous Compounds
  • Ferric Compounds