Resonant inelastic X-ray scattering determination of the electronic structure of oxyhemoglobin and its model complex
Year: 2019
Type: article
Abstract: Significance The electronic structure of the heme oxy-iron center in oxyhemoglobin and oxymyoglobin has been the subject of debate for decades. Various experimental and computational methods have been used to study this system, leading to conflicting conclusions. This study uses X-ray spectroscopy to directly probe the iron center in the highly delocalized oxyhemoglobin and its model compound to define the electronic structure and understand the differences between the protein and the model. This study settles a longstanding debate in bioinorganic chemistry and provides insight into heme iron–oxygen binding, the key first step in many biocatalytic processes.
Institutions: Stanford University, SLAC National Accelerator Laboratory, Stanford Synchrotron Radiation Lightsource, Centre National de la Recherche Scientifique, Université de Bourgogne, Institut de Chimie Moléculaire de l'Université de Bourgogne, Uppsala University, European Synchrotron Radiation Facility
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: green
Awards: G1229526393, G1286251239, G1804828992, G1831385526, G2300450775, G2371548206, G262532246, G303061748, G315621713, G3488436650, G3629260272, G4200735206, G4235786860, G4280418065, G4581610328, G4711507462, G495301720, G498139845, Spectroscopic Characterization of Oxygen Intermediates in Non-heme and Heme Iron Enzymes, G5570207115, G6550344761, G6703414148, G7283024673, A Synchroton Radiation Structural Biology Resource, G8382000481, G8925327636, G9000069621, G911061179, G969889393
OpenAlex ID: W2913342659