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 - art. no. 155501
S. Della Longa et al., 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 - art. no. 155501, PHYS REV L, 8715(15), 2001, pp. 5501
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-hem
e 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)degre
es.