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Resonant inelastic X-ray scattering determination of the electronic structure of oxyhemoglobin and its model complex.


ABSTRACT: Hemoglobin and myoglobin are oxygen-binding proteins with S = 0 heme {FeO2}8 active sites. The electronic structure of these sites has been the subject of much debate. This study utilizes Fe K-edge X-ray absorption spectroscopy (XAS) and 1s2p resonant inelastic X-ray scattering (RIXS) to study oxyhemoglobin and a related heme {FeO2}8 model compound, [(pfp)Fe(1-MeIm)(O2)] (pfp = meso-tetra(?,?,?,?-o-pivalamido-phenyl)porphyrin, or TpivPP, 1-MeIm = 1-methylimidazole) (pfpO2), which was previously analyzed using L-edge XAS. The K-edge XAS and RIXS data of pfpO2 and oxyhemoglobin are compared with the data for low-spin FeII and FeIII [Fe(tpp)(Im)2]0/+ (tpp = tetra-phenyl porphyrin) compounds, which serve as heme references. The X-ray data show that pfpO2 is similar to FeII, while oxyhemoglobin is qualitatively similar to FeIII, but with significant quantitative differences. Density-functional theory (DFT) calculations show that the difference between pfpO2 and oxyhemoglobin is due to a distal histidine H bond to O2 and the less hydrophobic environment in the protein, which lead to more backbonding into the O2 A valence bond configuration interaction multiplet model is used to analyze the RIXS data and show that pfpO2 is dominantly FeII with 6-8% FeIII character, while oxyhemoglobin has a very mixed wave function that has 50-77% FeIII character and a partially polarized Fe-O2 ?-bond.

SUBMITTER: Yan JJ 

PROVIDER: S-EPMC6386657 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Resonant inelastic X-ray scattering determination of the electronic structure of oxyhemoglobin and its model complex.

Yan James J JJ   Kroll Thomas T   Baker Michael L ML   Wilson Samuel A SA   Decréau Richard R   Lundberg Marcus M   Sokaras Dimosthenis D   Glatzel Pieter P   Hedman Britt B   Hodgson Keith O KO   Solomon Edward I EI  

Proceedings of the National Academy of Sciences of the United States of America 20190204 8


Hemoglobin and myoglobin are oxygen-binding proteins with S = 0 heme {FeO<sub>2</sub>}<sup>8</sup> active sites. The electronic structure of these sites has been the subject of much debate. This study utilizes Fe K-edge X-ray absorption spectroscopy (XAS) and 1s2p resonant inelastic X-ray scattering (RIXS) to study oxyhemoglobin and a related heme {FeO<sub>2</sub>}<sup>8</sup> model compound, [(pfp)Fe(1-MeIm)(O<sub>2</sub>)] (pfp = meso-tetra(α,α,α,α-<i>o</i>-pivalamido-phenyl)porphyrin, or Tpiv  ...[more]

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