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 . 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 includes a Fe-CO distance of , with a tilting angle between the heme normal and the Fe-C vector of , and a bending angle between the Fe-C vector and the C-O bond of .
- Received 13 April 2001
DOI:https://doi.org/10.1103/PhysRevLett.87.155501
©2001 American Physical Society