Features of the electronic structure of the active center of an HbS molecule

D. Yu Novoselov, Dm M. Korotin, V. I. Anisimov

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Features of the electronic structure of the nonprotein part of the mutant form of the human hemoglobin molecule, HbS, are studied along with the magnetic state of the iron ion that is the "nucleus" of the active center of the molecule. It is found that the mutant form of the HbS molecule differs from a normal hemoglobin molecule by the distortion of the local environment of the iron ion, which changes the energy level splitting by a crystal field. As a result of ab initio calculations, the magnetic transition in the iron atom from the high-spin state to the low-spin state upon the addition of molecular oxygen to hemoglobin molecule is reproduced. It is established for the first time that a change in the crystal and electronic structure of the active center as a result of a mutation can lead to a substantial change in the energy of the bond between the active center of the hemoglobin molecule and an oxygen molecule.

Original languageEnglish
Pages (from-to)113-116
Number of pages4
JournalRussian Journal of Physical Chemistry A
Volume90
Issue number1
DOIs
Publication statusPublished - 1 Jan 2016
Externally publishedYes

Keywords

  • bonding energy
  • electron structure
  • hemoglobin
  • spin transition

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