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Probing the electronic structure of the hemoglobin active center in physiological solutions.
Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Materials Science.
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2009 (English)In: Physical Review Letters, ISSN 0031-9007, E-ISSN 1079-7114, Vol. 102, no 6, 068103- p.Article in journal (Refereed) Published
Abstract [en]

Soft-x-ray absorption spectroscopy at the L_{2,3} 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.

Place, publisher, year, edition, pages
2009. Vol. 102, no 6, 068103- p.
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Physical Sciences
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URN: urn:nbn:se:uu:diva-150592ISI: 000263389500070PubMedID: 19257637OAI: oai:DiVA.org:uu-150592DiVA: diva2:407836
Available from: 2011-04-01 Created: 2011-04-01 Last updated: 2017-12-11Bibliographically approved

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