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 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.
Della Longa
S
S
Dipartimento Medicina Sperimentale, Università L'Aquila, 67100 L'Aquila, Italy.
Arcovito
A
A
Girasole
M
M
Hazemann
J L
JL
Benfatto
M
M
D000818:Animals; D001665:Binding Sites; D002248:Carbon Monoxide / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006418:Heme / Q000737:chemistry; D007501:Iron / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D010782:Photolysis; D011487:Protein Conformation; D012542:Scattering, Radiation; D013052:Spectrometry, X-Ray Emission; D014907:Whales
D009211:Myoglobin; C018013:carboxymyoglobin; D006418:Heme; D002248:Carbon Monoxide; D007501:Iron