Abstract
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 based on the full multiple scattering approach. The extracted local structure of Mb(*)CO includes a Fe-CO distance of (3.08+/-0.07) A, with a tilting angle between the heme normal and the Fe-C vector of (37+/-7) degrees, and a bending angle between the Fe-C vector and the C-O bond of (31+/-5) degrees.
| Lingua originale | Inglese |
|---|---|
| pagine (da-a) | 155501-155501 |
| Numero di pagine | 1 |
| Rivista | Physical Review Letters |
| Volume | 87 |
| Stato di pubblicazione | Pubblicato - 2001 |
Keywords
- Animals
- Binding Sites
- Carbon Monoxide
- Crystallography, X-Ray
- Heme
- Iron
- Myoglobin
- Photolysis
- Protein Conformation
- Scattering, Radiation
- Spectrometry, X-Ray Emission
- Whales
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