Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal

We report the first quantitative analysis of the Fe K-edge polarized x-ray absorption near edge structure of the iron protein carbonmonoxy-myoglobin (MbCO) single crystal and of its cryogenic photoproduct Mb(*)CO. The CO-Fe-heme local structure has been determined using a novel fitting procedure bas...

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Veröffentlicht in:	Physical review letters 2001-10, Vol.87 (15), p.155501-155501, Article 155501
Hauptverfasser:	Della Longa, S, Arcovito, A, Girasole, M, Hazemann, J L, Benfatto, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Carbon Monoxide - chemistry Crystallography, X-Ray Heme - chemistry Iron - chemistry Myoglobin - chemistry Photolysis Protein Conformation Scattering, Radiation Spectrometry, X-Ray Emission Whales
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