Probing the electronic structure of the hemoglobin active center in physiological solutions

Emad F. Aziz, Niklas Ottosson, Sébastien Bonhommeau, Nora Bergmann, Wolfgang Eberhardt, Majed Chergui

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Abstract

Soft-x-ray absorption spectroscopy at the L2,3 edge of the iron center in bovine hemoglobin and hemin under physiological conditions is reported for the first time. Spectra of the same compounds in solid form are presented for comparison. Striking differences in the electronic structure of the metalloporphyrin are observed between the liquid and solid compounds. We unambiguously show that hemoglobin and hemin are in a high-spin ferric state in solution, and that the 2p spin-orbit coupling decreases for hemin compared to the hemoglobin, while this is not the case in solids. The spectra were simulated using ligand field multiplet theory, in good agreement with the experiment, allowing quantification of the amount of charge transfer between the porphyrin and Fe3+ ion in hemoglobin and in hemin.

Original languageEnglish
Article number068103
JournalPhysical Review Letters
Volume102
Issue number6
DOIs
Publication statusPublished - 13 Feb 2009
Externally publishedYes

Cite this

Aziz, E. F., Ottosson, N., Bonhommeau, S., Bergmann, N., Eberhardt, W., & Chergui, M. (2009). Probing the electronic structure of the hemoglobin active center in physiological solutions. Physical Review Letters, 102(6), [068103]. https://doi.org/10.1103/PhysRevLett.102.068103