Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release

Journal Article (Review;Journal)

Desired mutations were successfully introduced to the N-lobe of human transferrin in which Glu, Gln, and Ala replaced His 249. The structural analysis of H249E mutant was successfully carried out and was compared with the wild type. The pH stability of the mutants and the kinetic stability of the Fe-mutant complexes were determined and were found to be in accordance with similar investigations carried out in the past.

Duke Authors

Cited Authors

  • Dhungana, S; Crumbliss, AL

Published Date

  • December 1, 2000

Published In

Volume / Issue

  • 13 / 12

Start / End Page

  • 770 - 775

International Standard Serial Number (ISSN)

  • 1431-9268

Citation Source

  • Scopus