Journal
PHYSICAL REVIEW LETTERS
Volume 87, Issue 15, Pages -Publisher
AMERICAN PHYSICAL SOC
DOI: 10.1103/PhysRevLett.87.155501
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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) Angstrom, 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.
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