Ligand Energy Controls the Heme-Fe Valence in Aqueous Myoglobins

書誌事項

公開日
2009
DOI
  • 10.1143/jpsj.78.044802
公開者
一般社団法人 日本物理学会

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説明

We use resonant X-ray emission spectroscopy and model calculations to quantify the ligand: heme-Fe energy structure of aqueous myoglobins. For reduced (Fe2+) and oxidized (Fe3+) states, the removal or addition of an electron primarily involves charge changes on the ligand-site, and not the Fe-site. The results indicate a finite positive/negative charge-transfer energy Δ between the heme-Fe 3d and ligand valence electronic states for Fe2+/Fe3+. Thus, the energy difference between the ligand and Fe 3d states (+Δ or −Δ) determines the charge properties of myoglobins. The study provides a reliable method for characterizing ligand-metal binding of biological systems in solution.

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